CYCLIC COMPOUNDS USEFUL AS INHIBITORS OF PLATELET GLYCOPROTEIN IIb/IIIa

Abstract: This invention relates to novel cyclic compounds containing carbocyclic ring systems useful as antagonists of the platelet glycoprotein IIb/IIIa complex, to pharmaceutical compositions containing such cyclic compounds, and to methods of using these compounds for the inhibition of platelet aggregation.

Description: TITLE Cyclic Compounds Useful as Inhibitors of Platelet Glycoprotein Ilb/IIIa F ELP QF THE INVE TION This invention relates to novel cyclic compounds containing carbocyclic ring systems useful as antagonists of the platelet glycoprotein Ilb/IIIa complex, to pharmaceutical compositions containing such cyclic compounds, and to methods of using these compounds for the inhibition of platelet aggregation. BACKGROUND OF THE INVENTION Activation of platelets and the resulting platelet aggregation and secretion of factors by the platelets have been associated with different pathophysiological conditions including cardiovascular and cerebrovascular thromboembolic disorders, for example, the thromboembolic disorders associated with unstable angina, myocardial infarction, transient ischemic attack, stroke, atherosclerosis and diabetes. The contribution of platelets to these disease processes stems from their ability to form aggregates, or platelet thrombi, especially in the arterial wall following injury. Platelets are known to play an essential role in the maintenance of hemostasis and in the pathogenesis of arterial thrombosis. Platelet activation has been shown to be enhanced during coronary thrombolysis which can lead to delayed reperfusion and reocclusion. Clinical studies with aspirin, ticlopidine and a monoclonal antibody for platelet glycoprotein Ilb/IIIa provide biochemical evidence for platelet involvement in unstable angina, early stage of acute myocardial infarction, transient ischemic attack, cerebral ischemia, and stroke. Platelets are activated by a wide variety of agonists resulting in platelet shape change, secretion of granular contents and aggregation. Aggregation of platelets serves to further focus clot formation by concentrating activated clotting factors in one site. Several endogenous agonists including adenosine diphosphate (ADP) , serotonin, arachidonic acid, thrombin, and collagen, have been identified. Because of the involvement of several endogenous agonists in activating platelet function and aggregation, an inhibitor which acts against all agonists would represent a more efficacious antiplatelet agent than currently available antiplatelet drugs, which are agonist-specific. Current antiplatelet drugs are effective against only one type of agonist; these include aspirin, which acts against arachidonic acid; ticlopidine, which acts against ADP; thromboxane A2 synthetase inhibitors or receptor antagonists, which act against throitiboxane A ; and hirudin, which acts against thrombin. Recently, a common pathway for all known agonists has been identified, namely platelet glycoprotein Ilb/IIIa complex (GPIIb/IIIa) , which is the membrane protein mediating platelet aggregation. A recent review of GPIIb/IIIa is provided by Phillips et al. (1991) Cell 65: 359-362. The development of a GPIIb/IIIa antagonist represents a promising new approach for antiplatelet therapy. Recent studies in man with a monoclonal antibody for GPIIb/IIIa indicate the antithrombotic benefit of a GPIIb/IIIa antagonist. There is presently a need for a GPIIb/IIIa-specific antiplatelet agent which inhibits the activation and aggregation of platelets in response to any agonist. Such an agent should represent a more efficacious antiplatelet therapy than the currently available agonist-specific platelet inhibitors. 5 GPIIb/IIIa does not bind soluble proteins on unstimulated platelets, but GPIIb/IIIa in activated * platelets is known to bind four soluble adhesive proteins, namely fibrinogen, von Willebrand factor, fibronectin, and vitronectin. The binding of fibrinogen 10 and von Willebrand factor to GPIIb/IIIa causes platelets to aggregate. The binding of fibrinogen is mediated in part by the Arg-Gly-Asp (RGD) recognition sequence which is common to the adhesive proteins that bind GPIIb/IIIa. Several RGD-containing peptides and related 15 compounds have been reported which block fibrinogen binding and prevent the formation of platelet thrombi. For example, see Cadroy et al. (1989) J. Clin. Invest. 84: 939-944; Klein et al. U.S. Patent 4,952,562, issued 8/28/90; European Patent Application EP 0319506 A; 20 European Patent Application EP 0422938 Al; European Patent Application EP 0422937 Al; European Patent Application EP 0341915 A2; PCT Patent Application WO 89/07609; PCT Patent Application WO 90/02751; PCT Patent Application WO 91/04247; and European Patent Application 25 EP 0343085 Al. In the present invention we use conformationally- constraining carbocyclic ring systems as templates for cyclizing peptides such that they have high affinity and selectivity for GPIIb/IIIa. 30 DETAILED DESCRIPTION OF THE INVENTION This invention is directed to novel compounds of the formula (I) : J M / \ 0=C NR 2 (R 22 (R 23 } < „ l C (R 21) R l } n , R 31 ( I) or a pharmaceutically acceptable salt or prodrug form thereof wherein: R 31 is a Cζ-Ci saturated, partially saturated, or aromatic carbocyclic ring system substituted with 0-2 R 10 ; or n" and n' are independently 0-3; R 1 and R 22 are independently selected from the following groups: hydrogen, Cι-C8 alkyl substituted with 0-2 R 11 , C2-C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6~ C 10 bicycloalkyl substituted with 0-2 R 11 , aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including at least one nitrogen, oxygen, or sulfur heteroatoms, =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 OR 13 , -OC(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 1 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13 , -SO3H, -S02R 13 , -SR 13 , -S(=0)R 13 , -S02NR 13 R 14 , -NR 13 R 14 , -NHC (=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , NO2, -C (=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxi e, boronic acid, -OCH2CO2H, 2- (1-morpholino) ethoxy; R 1 and R 21 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R22 and R 23 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 1 and R 2 , where R 21 is H, can alternatively join to form a 5-8 membered carbocyclic ring substituted with 0-2 Rl2; RH is selected from one or more of the following: =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 OR 13 , -0C(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C (=0) R 13 , -NR 1 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13 , -SO3H, -S02R 13 , -SR 13 , -S(=0)R 13 , -S02NR 13 R 14 , -NR 13 R 14 , -NHC (=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , NO2, -C (=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, -OCH2CO2H, 2- (1-morpholino) ethoxy, C1-C5 alkyl, C2-C4 alkenyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C2-C6 alkoxyalkyl, C3-C6 cycloalkoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, NO2, -S02R 13a . or -S(=0)R 13a ) aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including at least one nitrogen, oxygen, or sulfur atom; R 12 is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, C3-C 6 cycloalkoxy, -OC(=0)R 13 , -C(=0)R 13 ,-0C (=0)OR 13 , -OR 13 , -CH 2 OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 1 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 1 S02NR 13 R 14 , -NR 1 Sθ2R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -Sθ2NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, me hylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2-(1-morpholino)ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, N0 2 , or -S(=0)R 13a ) ; R 13 is H, C1-C7 alkyl, aryl, -(Cχ-C6 alkyl)aryl, or C3- CQ alkoxyalkyl; R 13a is C1-C7 alkyl, aryl, -(Ci-Cβ alkyl)aryl, or C3-C6 alkoxyalkyl; R 14 is OH, H, C1-C4 alkyl, or benzyl; R 21 and R 23 are independently selected from: hydrogen; C 1 -C 4 alkyl, optionally substituted with halogen; C 1 -C2 alkoxy; benzyl; R 2 is H or Ci-Cs alkyl; R 1 ^ is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , -C (=0)NHOR 13 , -C (=0)NHNR 13 R 14 , oxime, boronic acid, C 3 -C 6 cycloalkoxy, -OC(=0)R 13 , -C (=0)R 13 ,-OC (=0)OR 13 , -OR 13 , -CH2OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 1 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2- (1-morpholino)ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, N0 , or -S(=0)R l3a ); J is β-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 ) C (R 4 ) (R 5 )C (=0) -, wherein: R 3 is H or Ci-Ce alkyl; R 4 is H or C1-C3 alkyl; R5 hydrogen, C1-C8 alkyl substituted with 0-2 R 11 , C2-C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6~ClO bicycloalkyl substituted with 0-2 R 11 , aryl substituted with 0-2 R 12 , 5 a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms, =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , 10 -C(=0)R 13 , -C(=0)NR 13 R 14 , -CH 2 OR 13 , -OC(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -SR 13 , 15 -S(=0)R 13a , -S02NR 13 R 14 , -NR 13 R 14 , -NHC(=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , NO2, -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, -OCH2CO2H, 2-(1-morpholino)ethoxy, -SC(=NH)NHR 13 , N 3 , -Si(CH 3 ) 3 , (C 1 -C5 20 alkyl)NHR 16 ; -(C 0 -C 6 alkyl)X; independently 0,1; 30 -(CH2) m S(CH2)2X, where m = 1,2; wherein X is defined below; and R 3 and R 4 may also be taken together to form (CH 2 ) n X I "CH 2 CHCH 2 " , where R 3 and R^ can also be taken together to form -(CH2)t- ( = 2-4) or -CH 2 SC (CH 3 ) 2 ~; or R 4 and R^ can also be taken together to form -(CH2)u _ , where u = 2-5; R 16 is selected from: an amine protecting group; 1-2 amino acids; 1-2 amino acids substituted with an amine protecting group; is a D-isomer or L-isomer amino acid of structure -N(R β )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Ce alkyl; " 9? is selected from: -(C1-C 7 alkyl)X; independently 0,1; -(CH2)mO-(Cι-C alkyl)-X, where = 1,2; -(CH2)mS-(Cι-C alkyl)-X, where m = 1,2; and X is selected from: -SC(NH)-NH2; R6 and R 7 may also be taken together to form (CH 2 ) n X I R 13 ; is -Y(CH2)vC(=0)-, wherein: Y is NH, N(Cι-C3 alkyl), 0, or S; and v = 1,2; is a D-isomer or L-isomer amino acid of structure -NR 17 -CH(R 8 )C(=0)-, wherein: R 17 is H, C 1 -C3 alkyl; R 8 is -CH2C02R 13 ,-CH2S03R 13a , -CH (CH3) CO2R 13 , -S02NR 13 R 14 , -CH2-boronic acid, -CH2~tetrazole, -NHSO2CF3, -CONHNHSO2CF3, -PO(OR 13 ) 2 , -PO(OR 13 )R 13 , -CONHOR 13 , -Sθ2NH-heteroaryl, -CH 2 S02NH-heteroaryl, -S0 2 NHCOR 13 , -CH 2 S0 2 NHCOR 13 , -CONHS0 2 R 13a , -CH 2 C0NHSO 2 R 13a , -NHS02NHCOR 13a , -NHCONHS0 2 R 13 , -SO2NHCONR 13 . This invention includes those compounds above of the formula: K' L / \ M / \ 0=C NR 2 (R 22 (R 23 )CJ n .. „ C(R 21 )R 1 ) n , R 31 or a pharmaceutically acceptable salt or prodrug form thereof wherein: R 31 is a Cg-Ci 4 saturated, partially saturated, or.aromatic carbocyclic ring system substituted with 0-2 R 10 ; or n" and n* are independently 0-3; R 1 and R 22 are independently selected from the following groups: hydrogen, C1-C8 alkyl substituted with 0-2 R 11 , C2-C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6~Ci0 bicycloalkyl substituted with 0-2 R 11 , aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms, =0, F, Cl, Br, I, -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 OR 13 , -OC(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 Sθ2NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -SR 13 , -S(=0)R 13a , -S02NR 13 R 14 , -CH 2 NR 13 R 14 , -NR 13 R 14 , -NHC(=NH)NHR 13 , -C(=NH)NHR 13 , NO 2 ; R 1 and R 21 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 22 and R 23 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 1 and R 2 , where R 21 is H, can alternatively join to form a 5-8 membered carbocyclic ring substituted with 0-2 R 12 ; R 11 is selected from one or more of the following: =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CH 2 OR 13 , -0C(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 1 S02R 13a , -SO3H, -S02R 13a , -SR 13 , -S(=0)R 13 , -S02NR 13 R 14 , -CH2NR 13 R 14 , -NR 13 R 14 , -NHC (=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , N0 2 , C1-C5 alkyl, C2-C4 alkenyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C2-C6 alkoxyalkyl, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, NO 2 , -SO2R 13 , or -S(=0)R 13a ) aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms; s selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , hydroxamic acid, hydrazide, oxime, boronic acid, sulfonamide, formyl, C3-C6 cycloalkoxy, -OC(=0)R 13 , -C(=0)R 13 ,- OC(=0)OR 13 , -OR 13 , -CH 2 OR 13 , -NR 13 R 14 , -OC(=0)NR 1 R 14 , -NR 14 C(=0)R 13 , -NR 1 C (=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 1 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, Ci- C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2- (1-morpholino) ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, NO 2 , or -S(=0)R 13a ); R 13 is H, C1-C7 alkyl, aryl, -(Cχ-C6 alkyl)aryl, or C3- C6 alkoxyalkyl; R 14 is OH, H, C1-C4 alkyl, or benzyl; R 21 and R 23 are independently selected from: hydrogen; C 1 -C 4 alkyl, optionally substituted with halogen; C 1 -C2 alkoxy; benzyl; R 2 is H or Ci-Cs alkyl; R 1 ^ is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , hydroxamic acid, hydrazide, oxime, boronic acid, sulfonamide, formyl, C3-C6 cycloalkoxy, -0C(=0)R 13 , -C(=0)R 13 ,- OC(=0)OR 13 , -OR 13 , -CH2OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, Cχ~ C haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2- (1-morpholino) ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, NO 2 , or -S(=0)R 13a ); J is β-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 ) C (R 4 ) (R 5 ) C (=0) -, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, C1-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C1-C6 cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S NH 2 , (CH 2 ) S NHC(=NH) (NH 2 ) , (CH 2 ) S NHR 16 , where s = 3-5; R 3 and R5 can be taken together to form -(CH2)t~ (t = 2-4) or -CH 2 SC(CH 3 ) 2 -; or R 4 and R^ can be taken together to form -(CH2)u~, where u = 2-5; R 16 is selected from: an amine protecting group; 1-2 amino acids; 1-2 amino acids subtituted with an amine protecting group; K is a D-isomer or L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Ce alkyl; R 7 is selected from: ) q -X , where q is independently 0,1; -(CH2) O-(Cι-C alkyl) -X, where m = 1,2; -CCH2) m S-(Cι-C 4 alkyl) -X, where m = 1,2; and X is selected from: R 13 / -N(Rl 3 )R 13 , -C(-NH) (NH 2 ) , -SC (NH)-NH2; R6 and R 7 may also be taken together to form (CH 2 ) n X I -CH 2 CHCH 2 - / where R 13 . L is -Y(CH2)vC(=0)-, wherein: Y is NH, N(Cι-C 3 alkyl), 0, or S; and v = 1,2; M is a D-isomer or L-isomer amino acid of structure -NR 17 -CH(R 8 )C(=0)-, wherein: R 17 is H, C 1 -C 3 alkyl; R 8 is -CH2C02R 13 , -CH2S03R 13a , -CH (CH3 ) CO2R 13 , -S02NR 13 R 14 , -CH2-boronic acid, or -CH2- tetrazole . Included in the present invention are compounds above, wherein : R 31 is selected from the group consisting of: (a) a 6 membered saturated, partially saturated or aromatic carbocyclic ring substituted with 0-2 R 10 ; (b) a 8-11 membered saturated, partially saturated, or aromatic fused bicyclic carbocyclic ring substituted with 0-2 R 10 ; or (c) a 14 membered saturated, partially saturated, or aromatic fused tricyclic carbocyclic ring substituted with 0-2 R ! 0. The present invention includes compounds of formula (I) above wherein: R 31 is selected from the group consisting of: (a) a 6 membered saturated, partially saturated, or aromatic carbocyclic ring of formula: wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 R iO ; (b) a 10 membered saturated, partially saturated, or aromatic bicyclic carbocyclic ring of formula: , wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 R 10 ; (c) a 9 membered saturated, partially saturated, or aromatic bicyclic carbocyclic ring of formula: , wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 RlO. This invention includes compounds of formula I wherein: R 31 is selected from (the dashed bond may be a single or double bond) : or wherein R 31 may be substituted independently with 0-2 R 10 ; n" is 0 or 1; n' is 0-3. Preferred compounds of the present invention include compounds of Formula (I) , or a pharmaceutically acceptable salt or prodrug form thereof wherein: R 31 is selected from: wherein R 31 may be substituted independently with 0-2 R 10 ; n" is 0 or 1; n' is 0-2. R 1 and R 22 are independently selected from H, C1-C4 alkyl, phenyl, benzyl, phenyl-(C2-C4)alkyl, C 1 -C 4 alkoxy; R 21 and R 23 are independently H or C 1 -C 4 alkyl; R 2 is H or Ci-Cβ alkyl; R 1 ^ is H, Ci-Cβ alkyl, phenyl, halogen, or C 1 -C 4 alkoxy; J is β-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H or C 1 -C3 alkyl; R 5 is H, Ci-Cs alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, Ci-Cβ cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S X where X is -NH or -NHC(=NH) (NH 2 ) and s = 3-5; or R 3 and R5 can be taken together to form -(CH2) t ~ ( fc = 2-4) or -CH SC(CH 3 ) 2 -;or R 4 and R5 can be taken together to form - (CR2 ) ~ r where u = 2-5; K is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Cβ alkyl; R 7 is -(CH2) P NHC(=NH) (NH2), where p = 3-5; -(CH2) r X,where r = 4-6; (CH2) S(CH 2 )2X, where m = 1,2; -(C 3 -C7 alkyl)-N-(Cι-C 6 alkyl) ~(CH2)m-0-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; - _CH2)πrS-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2) ; or (CH 2 ) n X I R 6 and R 7 are taken together to form ~ CH 2 CHCH 2 - ^ where n = 0,1 and X is -NHC(=NH) (NH2) ; L is -Y(CH2) V C(=0)-, wherein: Y is NH, 0, or S; and v = 1,2; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2C02H,-CH2S03H, or -CH(CH3)CO2H; Preferred compounds of the invention are 1,3- disubstituted phenyl compounds of the formula (II) : wherein R 1 is H, C1-C4 alkyl, phenyl, benzyl, or phenyl- (C]_- C4)alkyl; R 2 is H or methyl; J is β-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 ) C (R 4 ) (R 5 ) C (=0)-, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, Cχ-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C1-C6 cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH2) S X where X is NH 2 or NHC(=NH) (NH 2 ) and s = 3-5; or R 3 and R5 can be taken together to form -CH2CH2CH2- ; or R 4 and R 5 can be taken together to form -(CH2) U ~, where u = 2-5; K is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is ' H or C1-C8 alkyl; R 7 is -(CH2)pNHC(=NH) (NH2), where p = 3-5; - (CH2) rX, where r = 4-6; -(CH2) m S(CH2)2X, where m = 1,2; -(C 3 -C 7 alkyl)-N-(Cι-C 6 alkyl) -(CH2)m-0-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; -CCH2)m-S-(Cι-C 4 alkyl)-NH-(Cι-C6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2) , provided that X is not -NH2 when r = 4; or (CH 2 ) n X I R 6 and R7 are taken together to form -CH 2 CHCH 2 -^ where n = 0,1 and X is -NHC(=NH) (NH2) ; L is -Y(CH2) V C(=0)-, wherein: Y is NH, 0, or S; and v = 1,2; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2C02H,-CH2S03H, or -CH(CH3)CO2H; Further preferred compounds of the invention are 1,3-disubstituted phenyl compounds of the formula (II) wherein: R 1 is H, C1-C4 alkyl, phenyl, benzyl, or phenyl- (C2- C4)alkyl; R 2 is H or methyl; J is β-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H; R 5 is H, C1-C8 alkyl, C3-C6 cycloalkyl, C3-C 6 cycloalkylmethyl, Ci-Cβ cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S X where X is NH 2 or NHC(=NH) (NH 2 ) and s = 3,4,5; or R 3 and R5 can be taken together to form -CH2CH2CH2-; K is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: Rδ is H or C 3 -C 8 alkyl; R 7 is -(CH2)pNHC(=NH) (NH2), where p = 3-4; ere q = 0, 1; - (CH2) r X, here r = 4-6; -(CH2) m S(CH2)2Xf where m = 1,2; -(C 4 -C 7 alkyl)-N-(Cι-C 6 alkyl) -(CH2)m-0-(Cι-C 4 alkyl)-NH-(Cι-C6 alkyl), where m = 1,2; -(CH2)m-S-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2) , provided that X is not -NH2 when r = 4; or is -YCH2C(=0)-, wherein: Y is NH or 0; M is an L-isomer amino acid of structure -NH- CH(R 8 )C(=0)-, wherein: R 8 is -CH2CO2H or -CH2SO3H. More preferred compounds of the present invention are compounds of formula (II) above, wherein: R 1 is H; R 2 is H; J is β-Ala or an L-isomer or D-isomer amino acid of formula -N(R 3 )CH(R 5 )C(=0)-, wherein: R 3 is H and R 5 is H, CH3, CH2CH3, CH(CH3)2. CH(CH 3 )CH 2 CH 3 , CH 2 CH 2 CH 3 , CH 2 CH 2 CH 2 CH 3 , CH 2 CH 2 SCH 3 , CH2CH(CH3)2, (CH 2 ) 4 NH 2 ; or R 3 is CH 3 and R 5 is H; or R 3 and R5 can be taken together to form -CH2CH2CH2- K is an L-isomer amino acid of formula -N(CH 3 )CH(R 7 )C(=0)-, wherein: R 7 is -(CH2)3NHC(=NH) (NH2) ; L is -NHCH2C(=0)-; and M is an L-isomer amino acid of formula -NHCH(CH 2 COOH)C(=0)-. Specifically preferred are the following compounds having IC 50 values of less than or equal to 100 μM for inhibiting the aggregation of platelets (as described below) : The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Pro; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ser; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R and R 2 are H; J is D-Lys; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is β-Ala; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is β—Ala; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Pro; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Phe; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is methyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is methyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is phenyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is phenyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (III) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is D-NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Phg; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ile; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Tyr; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Ala; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is Arg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeAmf; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Ala; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is CtMeAsp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val;; K is NMeArg; L is Gly; and M is βMeAsp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is NMeAsp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is D-Asp. The compound of formula (II) wherein R 1 is H; R 2 is CH3; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Abu; K is di-NMeOrn; L is Gly; and M is Asp. 0 A (V) The compound of formula (V) wherein n"=l; R 1 , R 2 , and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (V) wherein n"=0; R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VI) wherein R 2 and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R-^,R 2 , and R 1 -* are H; R 10a is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 1( ^ are H; R 10a is I; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 10 are H; R 10a is I; J is D-Abu; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ are H; R 10a is OMe; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R-^,R 2 , and R 1( ^ are H; R 10a is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R , and R 1 ^ 3 - are H; R 10 is Cl; J is D-Val; K is NMeArg;. L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 1 ^ 3 are H; R 10 is MeO; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 10a are H; R 10 is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp. (VIII) (IX) The compound of formula (VIII) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (IX) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. More specifically preferred are the following compounds of formula (I) , all of which have IC50 values of less than 1.0 μM for inhibiting the aggregation of platelets (as described below) . The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Pro; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Lys; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is β-Ala; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is methyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is methyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 is phenyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (III) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is D-NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Phg; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Ile; K is NMeArg; L is Gly; and M is Asp. The compound of formula (V) wherein n"=l; R 1 , R 2 , and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (V) wherein n"=0; R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp The compound of formula (VI) wherein R 2 and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R^-O.are H; R 10a is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R , and R 1 '-' are H; R 10a is I; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 1 ^ are H; R 10a is I; J is D-Abu; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 10 are H; R 1 a is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 10a are H; R 10 is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 1( ^ a are H; R 10 is MeO; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VII) wherein R^R 2 , and R 10a are H; R 10 is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Tyr; K is NMeArg; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeAmf; L is Gly; and M is Asp. The compound of formula (II) wherein R 1 and R 2 are H; J is D-Val;; K is NMeArg; L is Gly; and M is βMeAsp. The compound of formula (II) wherein R 1 is H; R 2 is CH3; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (III) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. The compound of formula (VIII) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. In the present invention it has been discovered that the compounds above are useful as inhibitors of glycoprotein Ilb/IIIa (GPIIb/IIIa) . As discussed above, GPIIb/IIIa mediates the process of platelet activation and aggregation. The compounds of the present invention inhibit the activation and aggregation of platelets induced by all known endogenous platelet agonists. The present invention also provides methods for the treatment of conditions involving platelet activation and aggregation, including cardiovascular and cerebrovascular thromboembolic disorders, including, for example, thromboembolic disorders associated with unstable angina, myocardial infarction, transient ischemic attack, stroke, atherosclerosis, and diabetes, by administering to a host in need of such treatment a pharmaceutically effective amount of the compounds described above. The compounds of the present invention are useful for inhibiting the binding of fibrinogen to blood platelets, inhibiting aggregation of blood platelets, treating thrombus formation or embolus formation, or preventing thrombus or embolus formation in a mammal. The compounds of the invention may be used as a medicament for blocking fibrinogen from acting at its receptor site in a mammal. The compounds of the present invention can also be co-administered with suitable anti-coagulant agents, such as heparin or warfarin, or anti-platelet agents, such as aspirin. The compounds of the present invention may also be combined with thrombolytic or fibrinolytic agents, such as plasminogen activators, anistreplase, urokinase, or streptokinase, to achieve synergistic effects in the treatment of thromboembolic disorders. GPIIb/IIIa is known to be overexpressed in metastatic tumor cells. The compounds of the present invention may also be useful for the treatment of metastatic cancer. The compounds herein described may have asymmetric centers. Unless otherwise indicated, all chiral, diastereomeric and racemic forms are included in the present invention. Many geometric isomers of olefins, C=N double bonds, and the like can also be present in the compounds described herein, and all such stable isomers are contemplated in the present invention. Two distinct isomers (cis and trans) of the peptide bond are known to occur; both can also be present in the compounds described herein, and all such stable isomers are contemplated in the present invention. Unless otherwise specifically noted, the L-isomer of the amino acid is used at positions J, K, L, and M of the compounds of the present invention. The D and L-isomers of a particular amino acid are designated herein using the conventional 3-letter abbreviation of the amino acid, as indicated by the following examples: D-Leu, D-Leu, L-Leu, or L-Leu. When any variable (for example, R 1 through R^, m, n, p, X, Y, etc.) occurs more than one time in any constituent or in any formula, its definition on each occurrence is independent of its definition at every other occurrence. Also, combinations of substituents and/or variables are permissible only if such combinations result in stable compounds. As used herein, "alkyl" is intended to include both branched and straight-chain saturated aliphatic hydrocarbon groups having the specified number of carbon atoms; "alkoxy" represents an alkyl group of indicated number of carbon atoms attached through an oxygen bridge; "cycloalkyl" is intended to include saturated ring groups, such as cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, cycloheptyl and cyclooctyl; and "biycloalkyl" is intended to include saturated bicyclic ring groups such as [3.3.Ojbicyclooctane, [4.3.Ojbicyclononane, [4. .OJbicyclodecane (decalin) , [2.2.2]bicyclooctane, and so forth. "Alkenyl" is intended to include hydrocarbon chains of either a straight or branched configuration and one or more unsaturated carbon-carbon bonds which may occur in any stable point along the chain, such as ethenyl, propenyl and the like; and "alkynyl" is intended to include hydrocarbon chains of either a straight or branched configuration and one or more triple carbon-carbon bonds which may occur in any stable point along the chain, such as ethynyl, propynyl and the like. "Halo" or "halogen" as used herein refers to fluoro, chloro, bromo and iodo; and "counterion" is used to represent a small, negatively charged species such as chloride, bromide, hydroxide, acetate, sulfate and the like. As used herein, "aryl" is intended to mean phenyl or naphthyl; "carbocyclic" is intended to mean any stable 5- to 7- membered monocyclic or bicyclic or 7- to 14-membered bicyclic or tricyclic carbon ring, any of which may be saturated, partially unsaturated, or aromatic. Examples of such carbocyles include, but are not limited to cyclopentyl, cyclohexyl, phenyl, biphenyl, naphthyl, indanyl or tetrahydronaphthyl (tetralin) . As used herein, the term "heterocycle" or "heterocyclic ring system" is intended to mean a stable 5- to 7- membered monocyclic or bicyclic or 7- to 10- membered bicyclic heterocyclic ring which may be saturated, partially unsaturated, or aromatic, and which consists of carbon atoms and from 1 to 3 heteroatoms selected from the group consisting of N, 0 and S and wherein the nitrogen and sulfur heteroatoms may optionally be oxidized, and the nitrogen may optionally be quaternized, and including any bicyclic group in which any of the above-defined heterocyclic rings is fused to a benzene ring. The heterocyclic ring may be attached to its pendant group at any heteroatom or carbon atom which results in a stable structure. The heterocyclic rings described herein may be substituted on carbon or on a nitrogen atom if the resulting compound is stable. Examples of such heterocycles include, but are not limited to, pyridyl, pyrimidinyl, furanyl, thienyl, pyrrolyl, pyrazolyl, imidazolyl, tetrazolyl, benzofuranyl, benzothiophenyl, indolyl, indolenyl, quinolinyl, isoquinolinyl or benzimidazolyl, piperidinyl, 4-piperidonyl, pyrrolidinyl, 2- pyrrolidonyl, pyrrolinyl, tetrahydrofuranyl, tetrahydroquinolinyl, tetrahydroisoquinolinyl, decahydroquinolinyl or octahydroisoquinolinyl. By "stable compound" or "stable structure" is meant herein a compound that is sufficiently robust to survive isolation to a useful degree of purity from a reaction mixture, and formulation into an efficacious therapeutic agent. The term "substituted", as used herein, means that an one or more hydrogen on the designated atom is replaced with a selection from the indicated group, provided that the designated atom's normal valency is not exceeded, and that the substitution results in a stable compound. As used herein, the term "amine protecting group" means any group known in the art of organic synthesis for the protection of amine groups. Such amine protecting groups include those listed in Greene, "Protective Groups in Organic Synthesis" John Wiley & Sons, New York (1981) and "The Peptides: Analysis, Sythesis, Biology, Vol. 3, Academic Press, New York (1981) , the disclosure of which is hereby incorporated by reference. Any amine protecting group known in the art can be used. Examples of amine protecting groups include, but are not limited to, the following: 1) acyl types such as formyl, trifluoroacetyl, phthalyl, and p-toluenesulfonyl; 2) aromatic carbamate types such as benzyloxycarbonyl (Cbz) and substituted benzyloxycarbonyls, 1-(p-biphenyl)-1- methylethoxycarbonyl, and 9-fluorenylmethyloxycarbonyl (Fmoc) ; 3) aliphatic carbamate types such as tert- butyloxycarbonyl (Boc) , ethoxycarbonyl, diisopropylmethoxycarbonyl, and allyloxycarbonyl; 4) cyclic alkyl carbamate types such as cyclopentyloxycarbonyl and adamantyloxycarbonyl; 5) alkyl types such as triphenylmethyl and benzyl; 6) trialkylsilane such as trimethylsilane; and 7) thiol containing types such as phenylthiocarbonyl and dithiasuccinoyl. As used herein, "pharmaceutically acceptable salts and prodrugs" refer to derivatives of the disclosed compounds that are modified by making acid or base salts, or by modifying functional groups present in the compounds in such a way that the modifications are cleaved, either in routine manipulation or in vivo, to the parent compounds. Examples include, but are not limited to: mineral or organic acid salts of basic residues such as amines; alkali or organic salts of acidic residues such as carboxylic acids; esters of carboxylates; acetate, formate and benzoate derivatives of alcohols and amines; and the like. Pharmaceutically acceptable salts of the compounds of the invention can be prepared by reacting the free acid or base forms of these compounds with a stoichiometric amount of the appropriate base or acid in water or in an organic solvent, or in a mixture of the two; generally, nonaqueous media like ether, ethyl acetate, ethanol, isopropanol, or acetonitrile are preferred. Lists of suitable salts are found in Remington's Pharmaceutical Sciences. 17th ed., Mack Publishing Company, Easton, PA, 1985, p. 1418, the disclosure of which is hereby incorporated by reference. The term "amino acid" as used herein means an organic compound containing both a basic amino group and an acidic carboxyl group. Included within this term are modified and unusual amino acids,such as those disclosed in, for example, Roberts and Vellaccio (1983) The Peptides. 5: 342-429, the teaching of which is hereby incorporated by reference. The term "amino acid residue" as used herein means that portion of an amino acid (as defined herein) that is present in a peptide or pseudopeptide. The term "peptide" as used herein means a linear compound that consists of two or more amino acids (as defined herein) that are linked by means of peptide or pseudopeptide bonds. The compounds of the present invention can be prepared in a number of ways well known to one skilled in the art of organic synthesis. Preferred methods include but are not limited to those methods described below. The following abbreviations are used herein: D-Abu D-2-aminobutyric acid β-Ala or bAla 3-aminopropionic acid Boc t-butyloxycarbonyl Boc-iodo-Mamb t-butyloxycarbonyl-3-aminomethyl-4-iodo- benzoic acid Boc-Mamb t-butyloxycarbonyl-3-aminomethylbenzoic acid Boc-ON [2- (tert-butyloxycarbonyloxylimino) -2- phenylacetonitrile Cl2Bzl dichlorobenzyl CBZ Carbobenzyloxy DCC dicyclohexylcarbodiinu.de DIEA diisopropylethylamine di-NMeOrn N- XMe-N-γMe-ornithine DMAP 4-dimethylaminopyridine HBTU 2- ( lH-Benzotriazol-1-yl) -1 , 1 , 3 , 3- tetramethyluronium hexafluorophosphate NMeArg or MeArg α-N-methyl arginine NMeAmf N-Methylaminomethylphenylalanine NMeAsp α-N-methyl aspartic acid NMeGly or MeGly N-methyl glycine NMe-Mamb N-methyl-3-aminomethylbenzoic acid NMM N-methylmorpholine OcHex O-cyclohexyl OBzl O-benzyl TBTU 2-(lH-Benzotriazol-1-yl)-1, 1,3,3- tetramethylurσnium tetrafluoroborate Tos tosyl The following conventional three-letter amino acid abbreviations are used herein; the conventional one- letter amino acid abbreviations are not used herein: Ala alanine Arg arginine Asn asparagine Asp aspartic acid Cys cysteine Gin glutamine Glu glutamic acid Gly glycine His histidine He isoleucine Leu leucine Lys lysine Met methionine Nle norleucine Phe phenylalanine Phg phenylglycine Pro proline Ser serine Thr threonine Trp tryptophan Tyr tyrosine Val valine Peptide Synthesis The compounds of the present invention can be synthesized using standard synthetic methods known to those skilled in the art. Generally, peptides are elongated by deprotecting the α-amine of the C-terminal residue and coupling the next suitably protected amino acid through a peptide linkage using the methods described. This deprotection and coupling procedure is repeated until the desired sequence is obtained. This coupling can be performed with the constituent amino acids in a stepwise fashion, or condensation of fragments (two to several amino acids) , or combination of both processes, or by solid phase peptide synthesis according to the method originally described by Merrifield, J. Am. Chem. Soc, 85, 2149-2154 (1963), the disclosure of which is hereby incorporated by reference. The compounds of the invention may also be synthesized using automated peptide synthesizing equipment. In addition to the foregoing, procedures for peptide synthesis are described in Stewart and Young, "Solid Phase Peptide Synthesis", 2nd ed, Pierce Chemical Co., Rockford, IL (1984) ; Gross, Meienhofer, Udenfriend, Eds., "The Peptides: Analysis, Synthesis, Biology, Vol. 1, 2, 3, 5, and 9, Academic Press, New York, (1980- 1987); Bodanszky, "Peptide Chemistry: A Practical Textbook", Springer-Verlag, New York (1988); and Bodanszky et al. "The Practice of Peptide Sythesis" Springer-Verlag, New York (1984), the disclosures of which are hereby incorporated by reference. The coupling between two amino acid derivatives, an amino acid and a peptide, two peptide fragments, or the cyclization of a peptide can be carried out using standard coupling procedures such as the azide method, mixed carbonic acid anhydride (isobutyl chloroformate) method, carbodiimide (dicyclohexylcarbodiimide, diisopropylcarbodiimide, or water-soluble carbodiimides) method, active ester (p-nitrophenyl ester, N- hydroxysuccinic imido ester) method, Woodward reagent K method, carbonyldiimidazole method, phosphorus reagents such as BOP-C1, or oxidation-reduction method. Some of these methods (especially the carbodiimide) can be enhanced by the addition of 1-hydroxybenzotriazole. These coupling reactions may be performed in either solution (liquid phase) or solid phase. The functional groups of the constituent amino acids must be protected during the coupling reactions to avoid undesired bonds being formed. The protecting groups that can be used are listed in Greene, "Protective Groups in Organic Synthesis" John Wiley & Sons, New York (1981) and "The Peptides: Analysis, Sythesis, Biology, Vol. 3, Academic Press, New York (1981), the disclosure of which is hereby incorporated by reference. The α-carboxyl group of the C-terminal residue is usually protected by an ester that can be cleaved to give the carboxylic acid. These protecting groups include: 1) alkyl esters such as methyl and t-butyl, 2) aryl esters such as benzyl and substituted benzyl, or 3) esters which can be cleaved by mild base treatment or mild reductive means such as trichloroethyl and phenacyl esters. In the solid phase case, the C-terminal amino acid is attached to an insoluble carrier (usually polystyrene) . These insoluble carriers contain a group which will react with the carboxyl group to form a bond which is stable to the elongation conditions but readily cleaved later. Examples of which are: oxime resin (DeGrado and Kaiser (1980) J. Orσ. Chem. 45, 1295-1300) chloro or bromomethyl resin, hydroxymethyl resin, and aminomethyl resin. Many of these resins are commercially available with the desired C-terminal amino acid already incorporated. The α-amino group of each amino acid must be protected. Any protecting group known in the art can be used. Examples of these are: 1) acyl types such as formyl, trifluoroacetyl, phthalyl, and p- toluenesulfonyl; 2) aromatic carbamate types such as benzyloxycarbonyl (Cbz) and substituted benzyloxycarbonyls, 1-(p-biphenyl)-1- methylethoxycarbonyl, and 9-fluorenylmethyloxycarbonyl (Fmoc) ; 3) aliphatic carbamate types such as tert- butyloxycarbonyl (Boc) , ethoxycarbonyl, diisopropylmethoxycarbonyl, and allyloxycarbonyl; 4) cyclic alkyl carbamate types such as cyclopentyloxycarbonyl and adamantyloxycarbonyl; 5) alkyl types such as triphenylmethyl and benzyl; 6) trialkylsilane such as trimethylsilane; and 7) thiol containing types such as phenylthiocarbonyl and dithiasuccinoyl. The preferred α-amino protecting group is either Boc or Fmoc. Many amino acid derivatives suitably protected for peptide synthesis are commercially available. The α-amino protecting group is cleaved prior to the coupling of the next amino acid. When the Boc group is used, the methods of choice are trifluoroacetic acid, neat or in dichloromethane, or HC1 in dioxane. The resulting ammonium salt is then neutralized either prior to the coupling or in situ with basic solutions such as aqueous buffers, or tertiary amines in dichloromethane or dimethylformamide. When the Fmoc group is used, the reagents of choice are piperidine or substituted piperidines in dimethylformamide, but any secondary amine or aqueous basic solutions can be used. The deprotection is carried out at a temperature between 0 °C and room temperature. Any of the amino acids bearing side chain functionalities must be protected during the preparation of the peptide using any of the above-identified groups . Those skilled in the art will appreciate that the selection and use of appropriate protecting groups for these side chain functionalities will depend upon the amino acid and presence of other protecting groups in the peptide. The selection of such a protecting group is important in that it must not be removed during the deprotection and coupling of the α-amino group. For example, when Boc is chosen for the α-amine protection the following protecting groups are acceptable: p-toluenesulfonyl (tosyl) moieties and nitro for arginine; benzyloxycarbonyl, substituted benzyloxycarbonyls, or tosyl for lysine; benzyl or alkyl esters such as cyclopentyl for glutamic and aspartic acids; benzyl ethers for serine and threonine; benzyl ethers, substituted benzyl ethers or 2- bromobenzyloxycarbonyl for tyrosine; p-methylbenzyl, p- methoxybenzyl, acetamidomethyl, benzyl, or t- butylsulfonyl for cysteine; and the indole of tryptophan can either be left unprotected or protected with a formyl group. When Fmoc is chosen for the α-amine protection usually tert-butyl based protecting groups are acceptable. For instance, Boc can be used for lysine, tert-butyl ether for serine, threonine and tyrosine, and tert-butyl ester for glutamic and aspartic acids. Once the elongation and cyclization of the peptide is completed all of the protecting groups are removed. For the liquid phase synthesis the protecting groups are removed in whatever manner as dictated by the choice of protecting groups. These procedures are well known to those skilled in the art. When a solid phase synthesis is used, the peptide should be removed from the resin without simultaneously removing protecting groups from functional groups that might interfere with the cyclization process. Thus, if the peptide is to be cyclized in solution, the cleavage conditions need to be chosen such that a free α- carboxylate and a free α-amino group are generated without simultaneously removing other protecting groups. Alternatively, the peptide may be removed from the resin by hydrazinolysis, and then coupled by the azide method. Another very convenient method involves the synthesis of peptides on an oxime resin, followed by intramolecular nucleophilic displacement from the resin, which generates a cyclic peptide (Osapay, Profit, and Taylor (1990) Tetrahedron Letters 43, 6121-6124) . When the oxime resin is employed, the Boc protection scheme is generally chosen. Then, the preferred method for removing side chain protecting groups generally involves treatment with anhydrous HF containing additives such as dimethyl sulfide, anisole, thioanisole, or p-cresol at 0 °C. The cleavage of the peptide can also be accomplished by other acid reagents such as trifluoromethanesulfonic acid/trifluoroacetic acid mixtures. Unusual amino acids used in this invention can be synthesized by standard methods familiar to those skilled in the art ("The Peptides: Analysis, Sythesis, Biology, Vol. 5, pp. 342-449, Academic Press, New York (1981)). N-Alkyl amino acids can be prepared using proceedures described in previously (Cheung et al., (1977) Can . J. Chem. 55, 906; Freidinger et all, (1982) J. Org. Chem. 48, 77 (1982)), which are incorporated here by reference. The compounds of the present invention may be prepared using the procedures further detailed below. Representative materials and methods that may be used in preparing the compounds of the invention are described further below. Manual solid phase peptide synthesis was performed in 25 mL polypropylene filtration tubes purchased from BioRad Inc. Oxime resin (substitution level = 0.96 mmol/g) was prepared according to published procedures (DeGrado and Kaiser (1980) J. Org. Chem. 45, 1295) . All chemicals and solvents (reagent grade) were used as supplied from the vendors cited without further purification. t-Butyloxycarbonyl (Boc) amino acids and other starting amino acids may be obtained commercially from Bachem Inc., Bachem Biosciences Inc. (Philadelphia, PA) , Advanced ChemTech (Louisville, KY) , Peninsula Laboratories (Belmont, CA) , or Sigma (St. Louis, MO). 2-(lH-Benzotriazol-1-yl)-1, 1,3,3-tetramethyluronium hexafluorophosphate (HBTU) and TBTU were purchased from Advanced ChemTech. N-methylmorpholine (NMM) , jn-cresol, D-2-aminobutyric acid (Abu) , trimethylacetylchloride, diisopropylethylamine (DIEA) , 3-cyanobenzoic acid and [2-(tert-butyloxycarbonyloxylimino)-phenylacetonitrile] (Boc-ON) were purchased from Aldrich Chemical Company. Dimethylformamide (DMF) , ethyl acetate, chloroform (CHCI3) , methanol (MeOH) , pyridine and hydrochloric acid (HC1) were obtained from Baker. Acetonitrile, dichloromethane (DCM) , acetic acid (HOAc) , trifluoroacetic acid (TFA) , ethyl ether, triethylamine, acetone, and magnesium sulfate were purchased from EM Science. Palladium on carbon catalyst (10% Pd) was purchased from Fluka Chemical Company. Absolute ethanol was obtained from Quantum Chemical Corporation. Thin layer chromatography (TLC) was performed on Silica Gel 60 F254 TLC plates (layer thickness 0.2 mm) which were purchased from EM Separations. TLC visualization was accomplished using UV light, iodine, and/or ninhydrin spray. Melting points were determined using a Thomas Hoover or Electrothermal 9200 melting point apparatus and are uncorrected. HPLC analyses were performed on either a Hewlett Packard 1090, Waters Delta Prep 3000, Rainin, or DuPont 8800 system. NMR spectra were recorded on a 300 MHz General Electric QE-300, Varian 300, or Varian 400 spectrometer. Fast atom bombardment mass spectrometry (FAB-MS) was performed on a VG Zab-E double-focusing mass spectrometer using a Xenon FAB gun as the ion source or a Finnigan MAT 8230. Synthesis of 3 and 4-substituted Boc-aminomethvlbenzoic Acid Derivatives 3 and 4-substituted Boc-aminomethylbenzoic acid derivatives useful as intermediates in the synthesis of the compounds of the invention are prepared using standard procedures, for example, as described in Tett. Lett . , 4393 (1975); Modern Synthetic Reactions, H.O. House (1972); or Harting et al. J. Am. Chem. Soc , 50: 3370 (1928), and as shown schematically below. .".-Ami nomet-.hylhpnzoif. aciri « H l 3-Cyanobenzoic acid ( 10 .0 g, 68 mmol) was dissolved in o 200 ml ethanol by heating in a 35-50 C water bath. Concentrated HC1 (6.12 ml, 201 mmol) was added and the solution was transferred to a 500 ml nitrogen-flushed round bottom flask containing palladium on carbon catalyst (1.05 g, 10% Pd/C) . The suspension was stirred under an atmosphere of hydrogen for 38 hours, filtered through a scintered glass funnel, and washed thoroughly with H2O. The ethanol was removed under reduced pressure and the remaining aqueous layer, which contained a white solid, was diluted to 250 ml with additional H2O. Ethyl ether (250 ml) was added and the suspension was transferred to a separatory funnel. Upon vigorous shaking, all solids dissolved and the aqueous layer was then washed two times with ether, evaporated under reduced pressure to a volume of 150 ml, and lyophilized to give the title compound (3- aminomethylbenzoic acid-HCl) (8.10 g, 64%) as a beige solid. 1 H NMR (D2O) 4.27 (s, 2H) , 7.60 (t, 1H) , 7.72 (d,lH), 8.06 (d, 2H) . t-Bu ylc.xvf-arhonyl-3-aminome hvlbenzoic Acid fBnr.-Mamh) The title compound was prepared according to a modification of standard procedures previously reported in the literature (Itoh, Hagiwara, and Kamiya (1975) Tett . Lett . , 4393). 3-Aminomethylbenzoic acid (hydrochloride salt) (3.0 g, 16.0 mmol) was dissolved in 60 ml H2θ. To this was added a solution of Boc-ON (4.33 g, 17.6 mmol) in 60 ml acetone followed by triethylamine (5.56 ml, 39.9 mmol). The solution turned yellow and the pH was adjusted to 9 (wet pH paper) by adding an additional 1.0 ml (7.2 mmol) triethylamine. The solution was stirred overnight at room temperature at which time the acetone was removed under reduced pressure and the remaining aqueous layer was washed three times with ether. The aqueous layer was then acidified to pH 2 with 2N HC1 and then extracted three times with ethyl acetate. The combined organic layers were washed three times with H2O, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. The material was recrystallized from ethyl acetate/ hexane to give two crops of the title compound (2.58 g, 64%) as an off- white solid. mp 123-125°C H NMR (CDCI3) 1.47 (s, 9 H), 4.38 (br s, 2 H) , 4.95 (br s, 1H) , 7.45 (t, 1H) , 7.55 (d, 1H), 8.02 (d, 2H) . -But.γloxycarbonyl-N-me hyl-3-aminome hylberι___.ic Acid .Bo(_-Mamb. The title compound can be prepared according to standard procedures, for examples, as disclosed in Olsen, J " . Org. Chem. (1970) 35: 1912), and as shown schematically below. BOC — NH Synthesis of Aminomethγlbenzoic Acid Analogs Intermediates of the formula below may be prepared using standard synthetic procedures, for example, as shown in the indicated reaction schemes shown below. For R = CH3, CH2CH3, CH2CH2CH3, CH2CH2CH2CH3, CH(CH3)2, C(CH3)3, CH(CH3)CH2CH3, benzyl, cyclopentyl, cyclohexyl; see Scheme 1. For R = CH3, CH2CH2CH2CH3, phenyl; see Scheme 2. For R = CH3, phenyl; see Scheme 3 and 4. Scheme 1 : Sr eme 2: 56 SUBSTITUTE SHEET Scheme 3 : H ° Scheme 4 (i> NH_OH.HCI/E.OH/P, r. (ϋ) Pd-C/EtOH/HCI C on./H 2 3- r1 '- . -butvloxvcarbonvl. amino1 thvlbenzoic acid (BOC-MeMAMB. The title compound for the purpose of this invention was prepared according to the Scheme 4 (above) . 3-Acetylbenzoic acid (0.50 g, 3 mmol), hydroxylamine hydrochloride (0.70 g, 10 mmol) and pyridine (0.70 ml, 9 mmol) were refluxed in 10 ml ethanol, for 2 h. Reaction mixture was concentrated, residue triturated with water, filtered and dried. Oxime was isolated as a white solid (0.51 g ; 94.4% yield). 1 HNMR (CD3OD) 7.45-8.30 (m, 4H) , 2.30(s, 3H) . MS (CH 4 -CI) [M+H-O] = 164. A solution of the oxime (0.51 g, 3 mmol) in ethanol, containing 10% Pd on carbon (1.5 g) and cone. HC1 (0.25 ml, 3 mmol) was hydrogena t e d at 30 psi H2 pressure in a Parr hydrogenator for 5 h. Catalyst was filtered and the filtrate concentrated. Residue was triturated with ether. Amine hydrochloride was isolated as a white solid (0.48 g ; 85.7% yield). ^-HNMR (CD3OD) 7.6-8.15(m, 4H) , 4.55(q, 1H) , 1.70(s, 3H) . MS [M+H] = 166. Amine hydrochloride (0.40 g, 2 mmol) was dissolved in 15 ml water. A solution of BOC-ON (0.52 g, 2.1 mmol) in 15 ml acetone was added, followed by the addition of triethylamine (0.8 ml, 6 mmol). Reaction was allowed to proceed for 20 h. Reaction mixture was concentrated, partitioned between ethyl acetate and water. Aqueous layer was acidified to pH 2 using 10% HC1 solution. Product was extracted in ethyl acetate, which after the usual work up and recrystallization from ethyl acetate/hexane, gave the title compound as a white solid (0.30 g ; 57% yield), m.p. 116-118° C. iHNM (CDCI3) 7.35-8.2 (m, 4H) , 4.6(bs, 1.5H) , 1.50(d, 3H), 1.40(s, 9H) . MS (NH3-CI) [M+NH4] = 283. -π '-. -b.- ylnxycarhonyl. amino .henzylbenzoic aciri .ROC-PhMAMR. The title compound for the purpose of this invention was prepared according to the Scheme 4 (above) , by the procedure similar to that for the methyl derivative. A solution of 3-benzoylbenzoic acid (2.00 g, 9 mmol), hydroxylamine hydrochloride (2.00 g, 29 mmol) and pyridine (2.00 ml, 25 mmol) in ethanol was refluxed for 12 h. After the usual extractive work up, white solid was obtained (2.41 g) . The product still contained traces of pyridine, but was used in the next step without further purification. The crude product (2.00 g, ~8 mmol) was dissolved in 200 ml ethanol. 10% Pd-C (2.00 g) and con. HCl (1.3 ml, 16 mmol) were added. Reaction mixture was hydrogenated at 30 psi for 1 h. The catalyst was filtered and the reaction mixture concentrated. Upon trituration of the residue with ether and drying under vacuum, amine hydrochloride was obtained as a white solid (2.12 g ; 97% yield). !HNMR (CD3OD) 7.4-8.15 (m, 10H) , 5.75 (s, IH) . MS (CH4-CI) [M+H-OH] = 211. Amine hydrochloride (1.00 g, 4 mmol) was converted to its BOC-derivative by a procedure similar to the methyl case. 0.60 g (48% yield) of the recrystallized (from ethanol/hexane) title compound was obtained as a white solid, .p. 190-192° C. 1 -HNMR (CD3OD) 7.2-8.0 (m, 10H) , 5.90 (2s, IH, 2 isomers), 1.40(s, 9H) . MS (NH3-CI) [M+NH4-C4H8] = 289 t-Butvloxvcarbonvl-D-2-aminobutyric Acid The title compound was prepared by a modification of procedures previously reported in the literature (Itoh, Hagiwara, and Kamiya (1975) Tett . Lett . , 4393), as shown in the scheme below. D-2-aminobutyrlc acid D-2-aminobutyric acid (1.0 g, 9.70 mmol) was dissolved in 20 ml H2O and a solution of Boc-ON (2.62 g, 10.6 mmol) in 20 ml acetone was added. A white precipitate formed which dissolved upon addition of triethylamine (3.37 ml, 24.2 mmol) to give a pale yellow solution (pH = 9, wet pH paper) . The solution was stirred at room temperature overnight at which time the acetone was removed under reduced pressure. The remaining aqueous layer was extracted with ether three times, acidified to pH 2 with concentrated HCl, and then extracted with ethyl acetate three times. The combined organic layers were dried over anhydrous magnesium sulfate and evaporated under reduced pressure to give t- butyloxycarbonyl-D-2-aminobutyric acid as an oil (2.05 g,greater than quantitative yield, contains solvent), which was used without further purification. ^H NMR (CDCI3) 0.98 (t, 3H), 1.45 (s, 9H) , 1.73 (m, IH) , 1.90 (m, IH), 4.29 (m, IH) , 5.05 ( , IH) . Synthesis of t-Butyloxvcarbonγl-3-aminophenvlace ic Acid t-Butyloxycarbonyl-3-aminophenylacetic acids useful as intermediates in the synthesis of the compounds of the invention are prepared using standard procedures, for example, as described in Collman and Groh (1982) J " . Am. Chem. Soc , 104: 1391, and as shown schematically below. t-Butγloxycarbonvl-3-aminophenylacetic Acid A solution of 3-aminophenylacetic acid (Aldrich, 10 g, 66 mmol), di-tert-butyl dicarbonate (15.8 g, 72 mmol), and DIEA (8.6 g, 66 mmol) in 50 ml of dichloromethane was stirred overnight at room temperature. The reaction mixture was concentrated, partitioned between dichloromethane-H2θ, the water layer was separated, acidified to pH 3 with IN HCl, and extracted with dichloromethane. The extracts were washed with H2O, brine, dried over anhydrous sodium sulfate, and evaporated to dryness under reduced pressure. This material was purified by recrystallization from heptane to provide the title compound (3.7 g, 22%) as a white solid, mp 105°C; !R NMR (CDCI3) 7.35 (s, IH) , 7.25 (m, 3H), 6.95 (m, IH) , 6.60 (br s, IH) , 3.65 (s, 2H) , 1.50 (s, 9H) . Synthesis of 4. 5. and ..-Substituted 3- Aminomethvlbenzoic Acid«HCl. and 4. 5. and 6-S._bstit.uted t-Butyloxγcarbonvl-3-aminomethvlbenzoic Acid Derivatives 4, 5, and 6-Substituted 3-aminomethylbenzoic acid»HCl, and 4, 5, and 6-substituted t- butyloxycarbonyl-3-aminomethylbenzoic acid derivatives useful as intermediates in the synthesis of the compounds of the invention are prepared using standard procedures, for example, as described in Felder et al Helv. Chim . Acta, 48: 259 (1965); de Diesbach Helv. Chim . Acta, 23: 1232 (1949); Truitt and Creagn J " . Org. Chem . , 27: 1066 (1962); or Sekiya et al Chem. Pharm . Bull . , 11: 551 (1963), and as shown schematically below. Synthesis of 4-Chloro-3-aminomethvlbenzoic Acid'HCl The title compound was prepared by modification of procedures previously reported in the literature (Felder et al (1965) Helv. Chim. Acta, 48: 259). To a solution of 4-chlorobenzoic acid (15.7 g, 100 mmol) in 150 ml of concentrated sulfuric acid was added N-hydroxymethyl dichloroacetamide (23.7 g, 150 mmol) in portions. The reaction mixture was stirred at room temperature for 2 days, poured onto 375 g of ice, stirred for 1 hour, the solid was collected by filtration, and washed with H2O. The moist solid was dissolved in 5% sodium bicarbonate solution, filtered, and acidified to pH 1 with concentrated HCl. The solid was collected by filtration, washed with H2O, and air-dryed overnight to give 4- chloro-3-dichloroacetylaminomethylbenzoic acid (26.2 g, 89%) as a white powder. A suspension of 4-chloro-3- dichloroacetylaminomethylbenzoic acid (26.2 g, 88 mmol) in 45 ml of acetic acid, 150 ml of concentrated HCl, and 150 ml of H2O was heated to reflux for 3 hours, filtered while hot, and allowed to cool to room temperature. The solid was collected by filtration, washed with ether, washed with acetone-ether, and air-dryed overnight to give the title compound (7.6 g, 39%) as off-white crystals, mp 278-9°C; λ H NMR (D6-DMSO) 13.40 (br s, IH) , 8.75 (br s, 3H) , 8.20 (s, IH) , 7.95 (dd, IH) , 7.70 (d, IH), 4.20 (br s, 2H) . t-B.-ty_oxγπarhony1-4-chloro-3-aminome hylbenzoic Acid A suspension of 4-chloro-3-aminomethylbenzoic acid»HCl (6.7 g, 30 mmol) and triethylamine (9.3 g, 92 mmol) in 50 ml of H2O, was added to a solution of Boc-ON (9.2 g, 38 mmol) in 50 ml of tetrahydrofuran cooled to 0°C. The reaction mixture was stirred at room temperature overnight, and the volatile compounds were removed by concentration under reduced pressure. The residue was diluted with H2O, washed with ether, acidified to pH 3 with IN HCl, and extracted with ethyl acetate. The extracts were washed with H2O, brine, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. This material was triturated with ether-hexane to provide the title compound (7.4 g, 87%) as a white powder, mp 159°C (dec) ; !H NMR (D6-DMSO) 13.20 (br s, IH) , 7.90 (s, IH) , 7.80 (dd, IH), 7.60 (br s, IH) , 7.55 (d, IH) , 4.20 (br d, 2H), 1.40 (s, 9H) . 4 and 6-Substituted t-But.yloxycarbnnyl-3- aminnmethylbenznir Acid Dsrivat.ives The compounds listed below were prepared using the general procedure described above for t- butyloxycarbonyl-4-chloro-3-aminomethylbenzoic acid. Synthesi s of 2-Aminomethγlbenzoic AcidΗCl and 2- Aminomethylphenylacetic AcidΗCl 2-Aminomethylbenzoic acid-HCl and 2- aminomethylphenylacetic acid-HCl useful as intermediates in the synthesis of the compounds of the invention are prepared using standard procedures, for example, as described in Naito et al J. Antibiotics, 30: 698 (1977); or Young and Sweet J. Am. Chem. Soc , 80: 800 (1958), and as shown schematically below. ?-Aminnm_1-. vlohpnylac_ti r Acid δ-Lanf m The title compound was prepared by modification of procedures previously reported in the literature (Naito et al. (1977) J. Antibiotics, 30: 698) . To an ice-cooled suspension of 2-indanone (10.8 g, 82 mmol) and azidotrimethylsilane (9.4 g, 82 mmol) in 115 ml of chloroform was added 25 ml of concentrated sulfuric acid at a rate to maintain the temperature between 30-40°C. After an additional 3 hours, the reaction mixture was poured onto ice, and the water layer was made basic with concentrated ammonium hydroxide. The chloroform layer was separated, washed with H2O, brine, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. This material was purified by subli ination (145°C, <1 mm), followed by recrystallization from benzene to give the title compound (5.4 g, 45%) as pale yellow crystals, mp 149- 150°C; !H NMR (CDCI3) 7.20 (m, 5H) , 4.50 (s, 2H) , 3.60 (s, 2H) . 2-Aminomethylphenylacetic Acid»HCl The title compound was prepared by modification of procedures previously reported in the literature (Naito et al. (1977) J. Antibiotics, 30: 698). A mixture of 2- aminomethylphenylacetic acid δ-lactam (6.4 g, 44 mmol) and 21 ml of 6N HCl was heated to reflux for 4 hours. The reaction mixture was treated with activated carbon (Norit A), filtered, evaporated to dryness, and the residual oil triturated with acetone. Filtration provided the title compound (5.5 g, 62%) as colorless crystals, mp 168°C (dec); 1 H NMR (D6-DMSO) 12.65 (br s, IH) , 8.35 (br s, 3H) , 7.50 (m, IH) , 7.35 (m, 3H) , 4.05 (ABq, 2H) , 3.80 (s, 2H) . 2-Am_nome hylbenzc.ic Acid γ-Lactam The title compound was prepared by modification of procedures previously reported in the literature (Danishefsky et al. (1975) J. Org. Chem. , 40: 796) . A mixture of methyl o-toluate (45 g, 33 mol) , N- 5 bromosuccinimide (57 g, 32 mol) , and dibenzoyl peroxide (0.64 g) in 175 ml of carbon tetrachloride was heated to reflux for 4 hours . The cooled reaction mixture was filtered, evaporated to dryness under reduced pressure, dissolv_i in 250 ml of methanol, and concentrated ammonium hydroxide (75 ml, 1.11 mol) was added. The reaction mixture was heated to reflux for 5 hours, concentrated, filtered, and the solid washed with H2O followed by ether. This material was purified by recrystallization from H2O to give the title compound (11.0 g, 26%) as a white solid, mp 150°C; ^-H NMR (CDCI3) 7.90 (d, IH) , 7.60 (t, IH) , 7.50 (t, 2H) , 7.00 (br s, IH) , 4.50 (s, 2H) . 2-Aminomethvlbenzoic Acid>HCl The title compound was prepared using the general procedure described above for 2-aminomethylphenylacetic acid«HCl. The lactam (3.5 g, 26 mmol) was converted to the title compound (2.4 g, 50%) as colorless crystals, mp 233°C (dec); ^-H NMR (D6-DMSO) 13.40 (br s, IH) , 8.35 (br s, 3H) , 8.05 (d, IH) , 7.60 (m, 3H) , 4.35 (br s, 2H) . Alternatives to Mamb: Other Cyclic Peptide Intermediates Alternatives to Mamb useful as carbocylic residues R 31 in the cyclic peptides of the invention include aminoalkyl- naphthoic acid and aminoalkyl-tetrahydronaphthoic acid residues. Representative aminoalkyl-naphthoic acid and aminoalkyl-tetrahydronaphthoic acid intermediates useful in * the synthesis of cyclic peptides of the present invention are described below. The synthesis of these intermediates is outlined below in Scheme 4a. Scheme 4a The title compound was prepared according to a modification of standard procedures previously reported in the literature (Earnest, I., Kalvoda, J., Rihs, G., and Mutter, M., Tett. Lett., Vol. 31, No. 28, pp 4011- 4014, 1990) . 67 in the literature (Earnest, I . , Kalvoda, J . , Rihs , G . , and Mutter, M. , Tett . Lett . , Vol . 31, No . 28, pp 4011- 4014 , 1990) . 8-Amino-S . 6. 7. 8-t rahydro-2-naphthoic Acid Hydrochloride (8) As shown below in Scheme 4a, 4-phenylbutyric acid (1) was converted to the ethyl ester (2) which was acylated via aluminum chloride and acetylchloride to give 4-acetylphenylbutyric acid ethyl ester (3) . This ester was subjected to saponification to give 4- acetylphenylbutyric acid (4) . Subsequently, the acetyl group was oxidized to give 4-carboxyphenylbutyric acid (5) which was converted to the l-tetralin-7-carboxylic acid (6) using aluminum chloride in a Friedel-Crafts cyclization with resonably high yield. At that point, the tetralone was split into two portions and some was converted to the oxime (7) using sodium acetate and hydroxylamine hydrochloride.The oxime was subjected to hydrogenolysis to give the racemic mixture of 8-amino- 5, 6, 1,8-tetrahydro-2-naphthoic acid as the hydrochloride (8) for use as an intermediate for incorporation into the cyclic peptide. Part A - A solution of 4-phenylbutyric acid (50.0 g, 0.3 mol) in ethanol (140 mL) with concentrated sulfuric acid (0.53 mL) was stirred at reflux over 5 hours. The cooled solution was poured into ice water and extracted with ethyl acetate. The combined organic layers were backwashed with brine, dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure to give 4-phenylbutyric acid ethyl ester (56.07 g, 0.29 mol, 97%) as a yellow liquid. X H NMR (CDCI 3 ) d 7.3-7.1 (m, 5H), 4.1 (q, 2H, J=7.1 Hz), 2.7 (t, 2H, J=7.7 Hz), 2 .3 (t , 2H,- J=7 . 5 Hz ) , 1 . 95 (quintet , 2H, J=7 . 5 Hz ) , 1 .25 (t , 3H, J=7 . 1 Hz) . Part B - To a solution of aluminum chloride (153 g, 1.15 mol), and acetyl chloride (38.5 mL, 42.5 g, 0.54 mol) in dichloromethane (1500 mL) was added, dropwise, a solution of 4-phenylbutyric acid ethyl ester (50.0 g, 0.26 mol) in dichloromethane (500 mL) . All was stirred at ambient temperature for 15 minutes. The solution was poured into cold concentrated hydrochloric acid (2000 mL) and then extracted with dichloromethane. The combined organic layers were backwashed with brine, dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure to give 4- acetylphenylbutyric acid ethyl ester (53.23 g, 0.23 mol, 88%) as a dark yellow liquid. 1 H NMR (CDC1 3 ) d 7.9 (d, 2H, J=8.1 Hz), 7.25 (d, 2H, J=8.4 Hz), 4.1 (q, 2H, J=7.1 Hz), 2.75 (t, 2H, J=7.6 Hz), 2.6 (s, 3H) , 2.35 (t, 2H, J=7.6 Hz), 2.0 (quintet, 2H, J=7.5 Hz), 1.25 (t, 3H, J=7.1 Hz) . Part C -To a solution of 4-acetylphenylbutyric acid ethyl ester (50.0 g, 0. ' 21 mol) in ethanol (1250 mL) was added, dropwise, a solution of sodium hydroxide (50.0 g) in water (1250 mL) . All was stirred at reflux over 4 hours. The solution was concentrated to half volume and then acidified to a pH equal to 1.0 using hydrochloric acid (IN) . The resulting precipitate was collected and washed with water to give 4-acetylphenylbutyric acid (53.76 g, 0.26 mol, 99%) as a white solid, mp = 50-52°C; X H NMR (CDCI3) d 7.9 (d, 2H, J=8.1 Hz), 7.25 (d, 2H, J=9.1 Hz), 2.75 (t, 2H, J=7.7 Hz), 2.6 (s, 3H) , 2.4 (t, 2H, J=7.3 Hz), 2.0 (quintet, 2H, J=7.4 Hz). Part D -To a solution of sodium hypochlorite (330 mL, 17.32 g, 0.234 mol) in a solution of sodium hydroxide (50%, 172 mL) , warmed to 55°C, was added, portionwise as a solid, 4-acetylphenylbutyric acid (16.0 g, 0.078 mol) while keeping the temperature between 60-70°C. All was stirred at 55°C over 20 hours. The cooled solution was quenched by the dropwise addition of a solution of sodium bisulfite (25%, 330 mL) . The mixture was then transferred to a beaker and acidified by the careful addition of concentrated hydrochloric acid. The resulting solid was collected, washed with water and dried, then triturated sequentially with chlorobutane and hexane to give 4-carboxyphenylbutyric acid (15.31 g, 0.074 mol, 95%) as a white solid, mp = 190-195°C; 1 H NMR (DMSO) d 12.55 (bs, IH) , 8.1 (s, IH) , 7.85 (d, 2H, J=8.1 Hz), 7.3 (d, 2H, J=8.1 Hz), 2.7 (t, 2H, J=7.5 Hz), 2.2 (t, 2H, J=7.4 Hz), 1.8 (quintet, 2H, J=7.5 Hz). Part E - A mixture of 4-carboxyphenylbutyric acid (10.40 g, 0.05 mol), aluminum chloride (33.34 g, 0.25 mol) and sodium chloride (2.90 g, 0.05 mol) was heated with continual stirring to 190°C over 30 minutes. As the mixture cooled to 60°C, cold hydrochloric acid (IN, 250 mL) was carefully added. The mixture was extracted with dichloromethane. The combined organic layers were backwashed with dilute hydrochloric acid and water, dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure. The resulting solid was triturated with chlorobutane to give l-tetralon-7- carboxylic acid (9.59 g, 0.05 mol, 100%) as a brown solid, mp = 210-215°C; λ R NMR (DMSO) d 8.4 (s, IH) , 8.1 (d, 2H, J=8.0 Hz), 7.5 (d, IH, J=7.9 Hz), 3.0 (t, 2H, J=6.0 Hz), 2.65 (t, 2H, J=6.6 Hz), 2.1 (quintet, 2H, J=6.3 Hz) . Part F - A solution of l-tetralon-7-carboxylic acid (1.0 g, 0.0053 mol) and sodium acetate (1.93 g, 0.024 mol) and hydroxylamine hydrochloride (1.11 g, 0.016 mol) in a mixture of methanol and water (1:1, 15 mL) was stirred at reflux over 4 hours . The mixture was cooled and then added was more water (50 mL) . The solid was collected, washed with water and dried, then triturated with hexane to give l-tetralonoxime-7-carboxylic acid (0.78 g, 0.0038 mol, 72%) as a white solid, mp = 205-215°C; X H NMR (DMSO) d 11.3 (s, 2H) , 8.4 (s, IH) , 7.8 (d, IH, J=7.7 Hz), 7.3 (d, IH, J=7.7 Hz), 2.8 (t, 2H, J=5.9 Hz), 2.7 (d, 2H, J=6.6 Hz), 1.9-1.7 (m, 2H) . Part G - A mixture of l-tetralonoxime-7-carboxylic acid (0.75 g, 0.0037 mol) in methanol (25 mL) with concentrated hydrochloric acid (0.54 mL, 0.20 g, 0.0056 mol) and palladium on carbon catalyst (0.10 g, 5% Pd/C) was shaken for 20 hours at ambient temperature under an atmosphere of hydrogen (60 psi) . The reaction mixture was filtered over Celite 8 and washed with methanol. The filtrate was evaporated to dryness under reduced pressure and the residue was purified by flash chromatography using hexane:ethyl acetate: :1:1 to give the racemic mixture of 8-amino-5, 6, 7, 8-tetrahydro-2- naphthoic acid hydrochloride (0.225 g, 0.001 mol. 27%) as a white solid, mp - 289-291°C; 1 H NMR (DMSO) d 8.55 (bs, 3H) , 8.2-8.1 (m, IH) , 7.85-7.8 (m, IH) , 7.35-7.25 (m, IH), 4.5 (m, IH) , 2.9-2.8 (m, 2H) , 2.1-1.9 (m, 3H) , 1.85-1.7 (m, IH) . N-(BOC.-8-Αminomethyl-5.6.7.8-tetrahγdro-?-naphthoic Acid (12) As shown below in Scheme 4a, the remaining tetralone was then converted to the methyl ester (9) . Using a procedure from Gregory, G.B. and Johnson, A.L, JOC, 1990, 55, 1479, the tetralone methyl ester (9) was converted, first, to the cyanohydrin by treatment with trimethylsilylcyanide and zinc iodide and then, via the in situ dehydration with phosphorous oxychloride in pyridine, to the methyl 8-cyano-5,6-dihydro-2-naphthoate (11) . This naphthoate was divided into two portions and some was subjected to hydrogenolysis, N-BOC-protection and saponification to give N-(BOC)-8-aminomethyl- 5,6,7,8-tetrahydro-2-naphthoic acid (12) as an intermediate for incorporation into the cyclic peptide. Part A - A mixture of l-tetralon-7-carboxylic acid (7.0 g, 0.037 mol) in methanol (13.6 mL, 10.8 g, 0.30 mol) with a catalytic amount of hydrochloriic acid (0.07 mL, 0.12 g, 0.0012 mol) was stirred at reflux over 5 hours. The cooled reaction mixture was poured into ice water and extracted with ethyl acetate. The combined organic layers were backwashed with water and brine, dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure. The resulting solid was purified by flash chromatography using hexane:ethyl acetate: :75:25. The resulting solid was triturated with hexane to give l-tetralon-7-carboxylic acid methyl ester (3.61 g, 0.018 mol, 49%) as a yellow solid, mp = 170- 172°C; R NMR (CDC1 3 ) d 8.7 (s, IH) , 8.15 (d, IH, J«8.1 Hz), 7.35 (d, IH, J-8.1 Hz), 3.95 (s, 3H) , 3.05 (d, 2H, J=6.1 Hz), 2.7 (t, 2H, J=6.4 Hz), 2.15 (quintet, 2H, J=6.2 Hz) . Part B - A solution of l-tetralon-7-carboxylic acid methyl ester (3.50 g, 0.017 mol), trimethylsilylcyanide (1.98 g, 0.02 mol) and zinc iodide (0.10 g) in benzene (20 mL) was stirred at ambient temperature over 15 hours. Then added, sequentially and dropwise, was pyridine (20 mL) and phosphorous oxychloride (4.0 mL, 6.55 g, 0.0425 mol). The reaction mixture was stirred at reflux over 1 hour then evaporated to dryness under reduced pressure. The residue was taken up in chloroform, backwashed with water, dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure to give methyl 8-cyano-5,6-dihydro-2- naphthoate (1.70 g, 0.008 mol, 47%) as a yellow solid. mp = 73-75°C; X H NMR (CDCI 3 ) d 8.0-7.9 (m, IH) , 7.3-7.2 (m, IH), 6.95 (t, IH, J=4.8 Hz), 3.95 (s, 3H) , 2.9 (t, 2H, J=8.3 Hz), 2.6-2.4 (m, 3H) Part C - A mixture of methyl 8-cyano-5,6-dihydro-2- naphthoate (0.80 g, 0.0038 mol) in methanol (25 mL) with concentrated hydrochloric acid (0.56 mL) and palladium on carbon catalyst (0.40 g, 5% Pd/C) was shaken for 20 hours at ambient temperature under an atmosphere of hydrogen (50 psi) . The reaction mixture was filtered over Celite and washed with methanol. The filtrate was evaporated to dryness under reduced pressure and the residue was triturated with hexane to give the racemic mixture of methyl 8-aminomethyl-5, 6,7,8-tetrahydro-2- naphthoate (0.80 g, 0.0037 mol, 97%) as a white solid. mp = 172-179°C; ^-H NMR (DMSO) d 8.2-8.0 (m, . 4H) , 7.9-7.7 (m, 6H) , 7.5-7.2 (m, 4H) , 3.9-3.8 (m, 7H) , 3.3-2.7(m, 10H) , 2.0-1.6 (m, 8H) . Part D - A solution of methyl 8-aminomethyl-5, 6,7,8- tetrahydro-2-naphthoate (0.78 g, 0.0036 mol) and triethylamine (0.55 mL, 0.40 g, 0.004 mol) in aqueous tetrahydrofuran (50%, 75 mL) was added, portionwise as a solid, 2-(tert-butoxycarbonyloxyimino) -2- phenylacetonitrile (0.99 g, 0.004 mol). All was stirred at ambient temperature over 3 hours. The solution was concentrated to half volume and extracted with diethylether. The aqueous layer was then acidified to a pH of 1.0 using hydrochloric acid (IN) and then extraced with ethyl acetate. The combined organic layers were dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure. The residue was purified by flash chromatography using hexane:ethyl acetate::8:2 to give methyl N-(BOC)-8-aminomethyl-5, 6,7,8-tetrahydro- 2-naphthoate (0.54 g, 0.0017 mol, 47%) as a white solid, mp = 72-80°C; 1 H NMR (DMSO) d 13.8 (s, IH) , 7.8-7.65 (m, 3H), 7.6-7.5 (m, 3H) , 7.25-7.20 ( , IH) , 7.15-7.05 (m, IH) , 3.9-3.8 (m, IH) , 3.2-2.8 (m, 4H) , 1.8-1.6 (m, 3H) , 1.4 (s, 6H) . Part E - To a solution of methyl N-(BOC)-8-aminomethyl- 5,6,7,8-tetrahydro-2-naphthoate (0.50 g, 0.0016 mol) in ethanol (12.5 mL) was added, dropwise, a solution of sodium hydroxide (0.50 g) in water (12.5 mL) . All was stirred a reflux over 4 hours. The reaction mixture was concentrated to half volume and then acidified to a pH equal to 1.0 using hydrochloric acid (IN) . The residue was puified by flash chromatography using a gradient of hexane:ethyl acetate::1:1 to ethyl acetate to ethyl acetate: methanol: :9:1 to give the racemic mixture of the title compound, N-(BOC)-2-aminomethyl-5, 6,7,8- tetrahydro-2-naphthoic acid (0.19 g, 0.00062 mol, 39%) as a white solid, mp = 172-176°C; K NMR (DMSO) d 7.8 (s, IH), 7.65 (d, IH, J=8.1 Hz), 7.15 (d, IH, J=8.1 Hz), 7.1-7.0 (m, IH), 3.2-3.1 (m, 2H) , 3.0-2.7 ( , 4H) , 1.8- 1.6 (m, 4H) , 1.4 (s, 9H) . N- . ROr . -B-aminom..thvl-2-naphthr. . f . am' .. ( 1 4 ) The remaining naphthoate (11) was treated with 2,3- dichloro-5, 6-dicyano-l,4-benzoquinone (DDQ) in dioxane to aromatize the adjacent ring to give the methyl 8- cyano-2-naphthoate (13) . Then, the nitrile was reduced via hydrogentation and the methyl ester saponified to the carboxylic acid. This acid was then N-BOC-protected to give N-(BOC)-8-aminomethyl-2-naphthoic acid (14) as an intermediate for incorporation into the cyclic peptide. Part A - A solution of methyl 8-cyano-5,6-dihydro-2- naphthoate (1.0 g, 0.0047 mol) and 2,3-dichloro-5, 6- dicyano-1, -benzoquinone (1.07 g, 0.0047 mol) in dioxane (50 mL) was stirred at 120°C over 16 hours. The reaction mixture was poured into ice water and extracted with ethyl acetate. The combined organic layers were dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure. The residue was purified by flash chromatography using ethyl acetate to give methyl 8-cyano-2-naphthoate (0.72 g, 0.0034 mol, 73%) as a tan solid, mp = 178-182°C; ^-H NMR (CDCI 3 ) d 8.95 (s, IH), 8.3-8.2 (m, IH) , 8.15-8.10 (m, IH) , 8.0-7.95 (m, 2H), 7.7-7.6 (m, IH) , 4.05 (s, IH) . Part B - A mixture of methyl 8-cyano-2-naphthoate (1.0 g, 0.0047 mol) in methanol (35 mL) with concentrated hydrochloric acid (0.69 mL) andpalladium on. carbon catalyst (0.20 g, 5% Pd/C) was shaken for 6 hours at ambient temperature under anatmosphere of hydrogen (50 psi) . The reaction mixture was filtered over Celite e and washed with methanol. The filtrate was evaporated to dryness under reduced pressure and the residue was triturated with hexane to give methyl 8-aminomethyl-2- naphthoate (0.76 g, 0.0035 mol, 75%) as an oil. 1 H NMR (DMSO) d 8.75 (s, IH) , 8.5 (bs, 2H) , 8.2-8.05 (m, 3H) , 7.75-7.70 ( , 2H) , 4.6 (s, 2H) , 3.95 (m, 3H) . Part C - To a solution of methyl 8-aminomethyl-2- naphthoate (0.75 g, 0.0035 mol) in dry tetrahydrofuran (50 mL) , cooled to 0°C, was added a solution of lithium hydroxide (0.5 M, 5.83 mL) . All was stirred at ambient temperature over 20 hours. Another aliquot of lithium hydroxide was added and all was stirred for an additional 20 hours. The solid was collected and the filtrate was evaporated to dryness under reduced pressure. The solids were triturated with diethyl ether to give 8-aminomethyl-2-naphthoic acid (0.67 g, 0.0033 mol, 95%) as a white solid, mp = 223-225°C; X H NMR (DMSO) d 8.6 (s, IH) , 8.1-7.9 (m, IH) , 7.8-7.7 (m, 4H) , 7.55-7.5 (m, IH) , 7,45-7.35 (m, 2H) , 4.2 (s, 2H) . Part D - A solution of 8-aminomethyl-2-naphthoic acid (0.50 g, 0.00025 mol) and triethylamine (0.038 mL, 0.028 g, 0.000275 mol) in aqueous tetrahydrofuran (50%, 5 mL) was added, portionwise as a solid, 2-(tert- butoxycarbonyloxyimino)-2-phenylacetonitrile (0.068 g, 0.000275 mol) . All was stirred at ambient temperature over 5 hours. The solution was concentrated to half volume and extracted with diethylether. The aqueous layer was then acidified to a pH of 1.0 using hydrochloric acid (IN) and then extraced with ethyl acetate. The combined organic layers were dried over anhydrous magnesium sulfate and evaporated to dryness under reduced pressure to give the title compound, N- (BOC)-8-aminomethyl-2-naphthoic acid (0.050 g, 0.00017 mol) as a white solid, mp = 190-191°C; X R NMR (DMSO) d 13.1 (bs, IH), 8.8 (s, IH), 8.0 (q, 2H, J=7.9 Hz), 7.9 (d, IH, J=8.1 Hz), 7.6 (t, IH, J=7.5 Hz), 7.65-7.55 (m, 2H), 4.6 (d, 2H, J=5.5 Hz), 1.4 (s, 9H) . Synthesis of Cyclic Peptides t-Butyloxycarbonyl-3-aminomethylbenzoic acid (Boc- Mamb) is coupled to oxime resin by a modification of the method described by DeGrado and Kaiser (1980) J. Org. Chem . 45, 1295 using 1 equivalent of the 3- aminomethylbenzoic acid (with respect to the substitution level of the resin) , 1 equivalent of HBTU, and 3 equivalent of NMM. Alternatively, Boc-Mamb (1 equivalent) may be coupled to the oxime resin using 1 equivalent each of DCC and DMAP in methylene chloride. Coupling times range from 15 to 96 hours. The substitution level is then determined using either the picric acid test (Sarin, Kent, Tarn, and Merrifield, (1981) Anal . Biochem. 117, 145-157) or the quantitative ninhydrin assay (Gisin (1972) Anal. Chim. Acta 58, 248- 249) . Unreacted oxime groups are blocked using 0.5 M trimethylacetylchloride / 0.5 M diisopropylethylamine in DMF for 2 hours. Deprotection of the Boc protecting group is accomplished using 25% TFA in DCM for 30 minutes. The remaining amino acids or amino acid derivatives are coupled using between a two and ten fold excess (based on the loading of the first amino acid or amino acid derivative) of the appropriate amino acid or amino acid derivatives and HBTU in approximately 8 ml of DMF. The resin is then neutralized in situ using 3 eq. of NMM (based on the amount of amino acid used) and the coupling times range from 1 hour to several days. The completeness of coupling is monitored by qualitative ninhydrin assay, or picric acid assay in cases where the amino acid was coupled to a secondary amine. Amino acids are recoupled if necessary based on these results. After the linear peptide had been assembled, the N- terminal Boc group is removed by treatment with 25% TFA in DCM for 30 minutes. The resin is then neutralized by treatment with 10% DIEA in DCM. Cyclization with concomitant cleavage of the peptide is accomplished using the method of Osapay and Taylor ( (1990) J. Am . Chem. Soc , 112, 6046) by suspending the resin in approximately 10 ml/g of DMF, adding one equivalent of HOAc (based on the loading of the first amino acid) , and stirring at 50-60 C for 60 to 72 hours. Following filtration through a scintered glass funnel, the DMF filtrate is evaporated, redissolved in HOAc or 1:1 acetonitrile: H2O, and lyophilized to obtain protected, cyclized material. Alternatively, the material may be dissolved in methanol and precipitated with ether to obtain the protected, cyclized material. This is then treated using standard procedures with anhydrous hydrogen fluoride (Stewart and Young (1984) "Solid Phase Peptide Synthesis", 2nd. edition. Pierce Chemical Co., 85) containing 1 ml/g _n-cresol or anisole as scavenger o at 0 C for 20 to 60 minutes to remove side chain protecting groups. The crude product may be purified by reversed-phase HPLC using a 2.5 cm preparative Vydac C18 column with a linear acetonitrile gradient containing 0.1% TFA to produce pure cyclized material. The following N-Ct-Boc-protected amino acids may be used for the syntheses: Boc-Arg(Tos) , Boc-N-α-MeArg(Tos) , Boc- Gly, Boc-As (OcHex) , Boc-3-aminomethyl-4-iodo-benzoic acid, Boc-D-Ile, Boc-NMeAsp(OcHex) , Boc-NMe-Mamb, Boc-D- Phg, Boc-D-Asp(OBzl) , Boc-L-Asp(OcHex) , Boc-αMe- Asp(OcHex), Boc-βMe-Asp(OcHex) , Boc-L-Ala, Boc-L-Pro, Boc-D-Nle, Boc-D-Leu, Boc-D-Val, Boc-D-2-aminobutyric acid (Boc-D-Abu) , Boc-Phe, Boc-D-Ser(Bzl) , Boc-D-Ala, Boc-3-aminomethylbenzoic acid (Boc-Mamb) , Boc-D-Lys(2- C1Z) , Boc-β-Ala, Boc-D-Pro, Boc-D-Phe, Boc-D- Tyr(Cl2Bzl), Boc-NMe-Amf(CBZ) , Boc-aminotetralin- carboxylic acid, Boc-aminomethylnaphthoic acid, Boc-4- aminomethylbenzoic acid, or Boc-NMeGly. The synthesis of the compounds of the invention is further exemplified below. The Tables below set forth representative compounds of the present invention. Example I cyclo-(Gly-NMeArg-Gly-Asp-Mamb) ; J = Gly, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO:l) The title compound was prepared using the general procedure described below for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.336 mmol scale to give the protected cyclic peptide (218 mg, 84%) . The peptide (200 mg) and 200 μL of m-cresol were o treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (158 mg, greater than quantitative yield; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 11% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (21% recovery, overall yield 16.3%) . Mass spectrum: M+H = 533.26. Example 2 cyclo-(D-Ala-NMeArg-Gly-Asp-Mamb) ; J = D-Ala, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described below for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . Recoupling of the Boc-N-MeArg(Tos) residue was found to be necessary. The peptide was prepared on a 0.244 mmol scale to give the protected cyclic peptide (117 mg, 61%) . The peptide (110 mg) and 110 μL of m- cresol were treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.25%/ min. gradient of 2 to 11% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid. Mass spectrum: M+H = 547.23. Example 3 cyclo-(D-Abu-NMeArg-Gly-Asp-Mamb) ; J = D-Abu, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described below for Example 4. The peptide was prepared on a 0.101 mmol scale to give the protected cyclic peptide (51 mg, 63%) . The peptide (43 mg) and 50 μL of jn-cresol were treated with anhydrous hydrogen o fluoride at 0 C for 30 minutes The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (23 mg, 68.7%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/min. gradient of 7 to 14% acetonitrile containing 0.1% trifluoroacetic acid and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (31% recovery; overall yield 12.4%). Mass spectrum: M+H = 561.46. Example 4 cyclo-(D-Val-NMeArg-Gly-Asp-Mamb) ; J = D-Val, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H To a 25 ml polypropylene tube fitted with a frit was added Boc-Mamb (0.126 g, 0.5 mmol) and 6 ml of DMF. To this was added HBTU (0.194 g, 0.5 mmol), oxime resin (0.52 g, substitution level = 0.96 mmol/g) , and N- methylmorpholine (0.165 ml, 1.50 mmol). The suspension was mixed at room temperature for 24 hours. The resin was then washed thoroughly (10-12 ml volumes) with DMF (3x) , MeOH (lx), DCM (3x) , MeOH (2x) and DCM (3x) . The substitution level was determined to be 0.389 mmol/g by quantitative ninhydrin assay. Unreacted oxime groups were blocked by treatment with 0.5 M trimethylacetylchloride/ 0.5M DIEA in DMF for 2 hours. The following steps were then performed: (Step 1) The resin was washed with DMF(3x), MeOH (lx) , DCM (3x) , MeOH (2x) , and DCM (3x) . (Step 2) The t-Boc group was deprotected using 25% TFA in DCM for 30 minutes. (Step 3) The resin was washed with DCM (3x) , MeOH (lx), DCM (2x) , MeOH (3x) and DMF(3x) (Step 4) Boc-Asp(OcHex) (0.613 g, 1.94 mmol), HBTU (0.753 g, 1.99 mmol), 8 ml of DMF, and N-methylmorpholine (0.642 ml, 5.84 mmol) were added to the resin and the reaction allowed to proceed for 2.5 hours. (Step 5) The coupling reaction was found to be complete as assessed by the qualitative ninhydrin assay. Steps 1-5 were repeated until the desired sequence had been attained. The coupling of Boc-D-Val to NMeArg was monitored by the picric acid test. After the linear peptide was assembled, the N- terminal t-Boc group was removed by treatment with 25% TFA in DCM (30 min.) The resin was washed thoroughly with DCM (3x) , MeOH (2x) and DCM (3x) , and then neutralized with 10% DIEA in DCM (2 x 1 min.) The resin was washed thoroughly with DCM (3x) and MeOH (3x) and then dried. Half of the resin (0.101 mmol) was cyclized by treating with 6 ml of DMF containing HOAc (5.8 μL, o 0.101 mmol) and heating at 50 C for 72 hours. The resin was then filtered through a scintered glass funnel and washed thoroughly with DMF. The DMF filtrate was evaporated to an oil, redissolved in 1:1 acetonitrile: H2O, and lyophilized to give the protected cyclic peptide (49 mg, 60%) . The peptide (42 mg) was treated o with anhydrous hydrogen fluoride at 0 C, in the presence of 50 μL of m-cresol as scavenger, for 30 minutes to remove side chain protecting groups . The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (23 m , 70%; calculated as the acetate salt) . Purification was accomplished using reversed-phase HPLC with a preparative Vydac C18 column (2.5 cm) and a 0.23%/ minute gradient of 7 to 18% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound as a fluffy white solid (24% recovery; overall yield 9.4%); FAB-MS: [M+H] = 575.45. Solution Phase Synthesis of Example 4 The following abbreviations are used below for TLC solvent systems: chloroform/methanol 95:5 = CM; chloroform/acetic acid 95:5 = CA; chloroform/methanol/acetic acid 95:5 = CMA BocNMeArg (Tos) -Gly-OBzl — 25 mmol BocNMeArg (Tos) (11.07 g, Bachem), 30 mmol Gly-OBzl tosylate (10.10 g, Bachem), 25 mmol HBTU (0-Benzotriazole-N,N,N',N',- tetramethyl-uronium-hexafluorophosphate; 9.48 g; Advanced Chemtech) , and 75 mmol DIEA (diisopropylethylamine; Aldrich) were dissolved in 25 ml CH 2 CI 2 . The reaction was allowed to proceed 1 hr, the solvent was evaporated under reduced pressure at 50° to a syrup, wich was dissolved in 400 ml ethyl acetate. This solution was extracted with (150 ml each) 2 x 5% citric acid, 1 x water, 2 x sat. NaHCθ 3 , 1 x sat. NaCl. The organic layer was dried over MgSO_ι, and the solvent evaporated under reduced pressure. The resulting oil was triturated with petroleum ether and dried under high vacuum for a minimum of 1 hr. yield 14.7 g (99.5%); TLC R f( CM ) = 0.18 R f ( CA ) - 0.10; NMR is consistent with structure; FABMS M+H + = 590.43 (expected 590.26). NMeArg (Tos) -Gly-OBzl — 14.5 g (BocNMeArg(Tos)-Gly-OBzl (24.5 mmol) was dissolved in 30 ml TFA, allowed to react for 5 min., and the solvent evaporated at 1 mm mecury pressure at r.t. The resulting syrup was dissolved in 400 ml ice cold ethyl acetate, and extracted with 100 ml ice cold sat. NaHC03, the aqueous phase was extracted- twice with 200 ml ethyl acetate, and the combined organic phases were extracted once with 25 ml sat. NaCl. The solvent was evaporated under reduced pressure giving a viscous oil that was triturated with 300 ml ether. The resulting solid was filtered and washed with ether, giving a hydroscopic compound that was dried in a vacuum desiccator: yield 10.33 g (86.2%); TLC R f ( CM ) = 0.03; R f ( CMA ) = 0.20; NMR is consistent with structure; FABMS M+H+ = 490.21 (expected 490.20). Boc-D-Val-NMeArg (Tos) -Gly-OBzl — 9.80 mmol NMeArg(Tos)-Gly-OBzl (4.80 g), 9.82 mmol Boc-D-Val (2.13 g, Bachem), and 10.0 mmol HBTU (3.79 g) were dissolved in 10 ml methylene chloride. The flask was placed on an ice bath, and 20 mmol DIEA (3.48 ml) was added. The reaction was allowed to proceed at 0° for 15 min and 2 days at r.t. The reaction mixture was diluted with 400 ml ethyl acetate, extracted (200 ml each) 2 5% citric acid, 1 x sat. NaCl, dried over MgS0 and evaporated under reduced pressure. The resulting oil was triturated with 50, then 30 ml ether for 30 min with efficient mixing: yield 4.58 g (69%); TLC R f ( CM ) = 0- 27 (also contains a spot near the origin, which is an aromatic impurity that is removed during trituration of the product in the next step) ; NMR is consistent with structure; FABMS M+H + = 689.59 (expected 689.43). Boc-D-Val-NMeArg (Tos) -Gly — 4.50 g Boc-D-Val- NMeArg(Tos)-Gly-OBzl (4.44 mmol) dissolved in 80 ml methanol was purged with N 2 for 10 min. 1.30 g Pd/C catalyst (10% Fluka lot #273890) was then added, and then H 2 was passed directly over the surface of the reaction. TLC showed the reaction to be complete within approximately 0.5 hr. After 1 hr. the catalyst was removed by filtering through a bed of Celite, and the solvent removed at 40° under reduced pressure. The resulting solid was triturated well with 50 ml refluxing ether, filtered, and washed with petroleum ether: yield 3.05 g (78%); TLC R f CM ) = 0.03; R f ( CMA ) = 0.37; NMR is consistent with structure; FABMS M+H + = 599.45 (expected 599.29) . 4-Nitrobenzophenone Oxime (Ox) — 50 g 4- nitrobenzophenone (220 mmol, Aldrich) and 30.6 g hydroxylamine hydrochloride (Aldrich, 440 mmol) were heated at reflux in 0.5 L methanol/pyridine (9:1) for 1 hr. The reaction mixture was evaporated under reduced pressure, dissolved in 500 ml ether, and extracted with 200 ml each of 5% citric acid (2 times) and sat. NaCl (1 time) , dried over MgS0 4 , evaporated under reduced pressure and triturated with ether giving 44.35 g (83%) of the oxime as a mixture of the cis and trans isomers: TLC R f ( CM ) = 0.50; R f ( CMA ) = 0.82; NMR is consistent with structure; FABMS M+H + = 242.07 (expected 242.07) . BocMamb-Ox — 22 mmol BocMamb (5.522 g) , 20 mmol nitrobenzophenone oxime (4.84 g) , and 20 mmol DMAP (4- dimethylaminopyridine; Aldrich) were dissolved in 40 ml CH 2 CI 2 • The flask was placed on an ice bath, and 21 mmol DCC (Dicyclohexylcarbodiimide; 4.33 g) was added. The reaction was allowed to proceed on ice for 30 min and at r.t. over night. The dicyclohexylurea formed was filtered, and washed with 40 ml methylene chloride. The filtrate was evaporated under reduced pressure at r.t. to a syrup, and dissolved in 400 ml ethyl acetate. This solution was extracted with (150 ml each) 2 x 5% citric acid, 1 x water, 2 x sat. NaHCθ 3 , 1 x sat. NaCl. The organic layer was dried over MgS0 4 , and the solvent evaporated under reduced pressure. The resulting oil was triturated with petroleum ether and dried under high vacuum for a minimum of 1 hr. : yield 7.51 g (79%); TLC R f ( CM ) - 0.41; R f ( CMA ) = 0.66; NMR is consistent with structure; FABMS M+H + = 476.30 (expected 476.18). TFA-MAMB-Ox — BocMamb-Ox , 7.4 g (15.5 mmol) was dissolved in 30 ml methylene chloride plus 10 ml TFA (25% TFA) . The reaction was allowed to proceed at r.t. for 1 hr, and the solvent evaporated under reduced pressure at r.t. for 10 min, then at 40° for 15 min. The resulting syrup was triturated with ether (200 ml) at -5°, giving. The resulting crystals were filtered after 1 hr and washed well with ether: yield 7.22 g (95%); R f ( CMA ) = 0.25; NMR is consistent with structure; FABMS M+H + = 376.22 (expected 376.12). Boc-Asp (OcHex) -Ma b-Ox — 20 mmol Boc-Asp(OcHex) (6.308 g, Bachem) and 44 mmol DIEA (7.66 ml) were dissolved in 20 ml DMF. 20 mmol HBTU (7.58 g, Advanced Chemtech) was added, and the reaction allowed to proceed for 2 minutes with vigorous stirring. TFA-Mamb-Ox (7.13 g, 15 mmol) was added, and the reaction allowed to proceed o.n. at r.t. The solvent was removed under reduced pressure giving an oil, which was dissolved in 500 ml ethyl acetate, and this solution was extracted with (150 ml each) 2 x 5% citric acid, 1 x water, 2 x sat. NaHCθ 3 , 1 x sat. NaCl. The organic layer was dried over MgS0 , and the solvent evaporated under reduced pressure. The resulting oil was triturated with petroleum ether and dried under high vacuum: yield 9.76 g (97%); TLC R f ( CM ) = 0.55; NMR is consistent with structure; FABMS M+H + = 673.45 (expected 673.23). TFA Asp (OcHex) -MAMB-Ox — 15 mmol Boc-Asp(OcHex)-MAMB- Ox was dissolved in 50 ml 35% TFA in CH 2 CI 2 , and allowed to react 90 min. The solvent was evaporated under reduced pressure at r.t. for 10 min, then at 40° for 15 min. To remove traces of TFA, 25 ml DMF was added and the solvent evaporated at 50°. The resulting syrup was triturated with ether (200 ml) , then dried under high vacuum: yield 9.61 g (93%); R f ( CMA ) = 0.45; NMR is consistent with structure; FABMS M+H + = 573.56 (expected 573.23) . Boc-D-Val-NMeArg (Tos) -Gly-Asp (OcHex) -MAMB-Ox 10.0 mmol each TFA Asp(OcHex)-MAMB-Ox, Boc-D-Val-NMeArg(Tos)-Gly, and HBTU, plus 30 mmol DIEA were dissolved in 20 ml DMF. After 4 hr., the solvent was removed under reduced pressure, and the residue taken up in 600 ml ethyl acetate, which was extracted with 300 ml each of 5% citric acid, water and sat. NaCl. The organic layer was dried over MgSθ 4 , evaporated under reduced pressure, triturated with ether and dried in vacuo: yield 9.90 g (86%); R f ( CM ) = 0.10; NMR is consistent with structure; FABMS M+H + = 1153.22 (expected 1153.47) . TFA- D-Val-NMeArg (Tos) -Gly-Asp (OcHex) -MAMB-Ox This compound was prepared from Boc-D-Val-NMeArg(Tos)-Gly- Asp(OcHex)-MAMB-Ox (9.8 g, 8.5 mmol) by treatment with TFA/CH 2 CI 2 (1:1) for 45 min. The solvent was evaporated and the product triturated with ether: yield 9.73 g (98%); R f ( CM ) = 0.10; NMR is consistent with structure; FABMS M+H + = 1053.22 (expected 1053.4). cyclo ( • D-Val-NMeArg (Tos) -Gly-Asp (OcHex) -MAMB) TFA-D- Val-NMeArg(Tos)-Gly-Asp(OcHex)-MAMB-Ox (1.80 g, 1.54 mmol) , and 2 mmol each of DIEA and acetic acid were dissolved in 200 ml DMF. The mixture was heated to 50° for 2 days, then evaporated under reduced pressure. The syrup was dissolved in 400 ml ethyl acetate/n-butanol (1:1), and extracted with 200 ml each of 5% citric acid (3x) and sat. NaCl (lx) . The organic layer was dried over MgS0 4 and triturated twice with 200 ml ether: yield 1.07 g (86%); R f ( CM ) = 0.10; NMR is consistent with structure; FABMS M+H + = 811.2 " (expected 811.38). cyclo (-D-Val-NMeArg-Gly-Asp-MAMB) 0.50 g cyclo (D-Val- NMeArg(Tos)-Gly-Asp(OcHex)-MAMB) was treated with 5 ml HF at 0°C, in the presence of 0.5 ml of anisole for 30 min. The HF was removed under reduced pressure and the crude peptide triturated with ether, ethyl acetate and ether. The resulting solid was dissolved in 10% acetic acid and lyophilized: yield 0.321 g (82% calculated as the acetate salt) . The product was purified with a recovery of approximately 40% using the same method as described for the material synthesized by the solid phase procedure. Example 4b cyclo-(D-Val-D-NMeArg-Gly-Asp-Mamb) ; J = D-Val, K = D- NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val-NMeArg-Gly-Asp- Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.596 mmol scale to give the protected cyclic peptide (186 mg, 38.6%). The peptide (183 mg) and 0.183 mL of anisole were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (145 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (14.8% recovery, overall yield 5.3%); FAB-MS: [M+H] = 575.31. Example 5 cyclo-(D-Leu-NMeArg-Gly-Asp-Mamb) ; J = D-Leu, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.115 mmol scale to give the protected cyclic peptide (92.4 mg. 98%) . The peptide (92.4 mg) and 93 μL of _n-cresol were treated with anhydrous hydrogen fluoride at 0°C for 20 minutes. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (45.7 mg, 63%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 21% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (29% recovery, overall yield 16.5%) ;FAB-MS: [M+H] = = 589.48. Example 7 cyclo-(D-Nle-NMeArg-Gly-Asp-Mamb) ; J = D-Nle, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.586 mmol scale to give the protected cyclic peptide (305 mg, 63.3%). The peptide (295 mg) and 0.295 mL of anisole were treated with anhydrous hydrogen o fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (207 mg, 95.4%; calculated as the fluoride salt) . Purification was accomplished by reversed- phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 5.4 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (44% recovery, overall yield 22.9%); FAB-MS: [M+H] = 589.26. Example 11 cyclo-(D-Phg-NMeArg-Gly-Asp-Mamb) ; J = D-Phg, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val-NMeArg-Gly-Asp- Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (296 mg, 57.4%). The peptide (286 mg) and 0.286 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (210 mg, 98.9%; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 5.4 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (24.2% recovery, overall yield 11.9%); FAB¬ MS: [M+H] - 609.27. Example 12 cyclo-(D-Phe-NMeArg-Gly-Asp-Mamb) ; J = D-Phe, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val-NMeArg-Gly-Asp- Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (140 mg, 26.7%). The peptide (135 mg) and 0.135 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (108 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7.2 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (35% recovery, overall yield 8.7%); FAB-MS: [M+H] = 623.28. Example I3f cyclo-(D-Lys-NMeArg-Gly-Asp-Mamb) ; J = D-Lys, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.586 mmol scale to give the protected cyclic peptide (349 mg, 58.9%). The peptide (334 mg) and 334 μL of anisole were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound as a pale yellow solid (168 mg, 79.1%; calculated as the difluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 5.4 to 14.4% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (33.6% recovery, overall yield 12.1%); FAB-MS: [M+H] = 604.32 Example 13r cyclo-(D-Ile-NMeArg-Gly-Asp-Mamb) ; J = D-Ile, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val-NMeArg-Gly-Asp- Ma b) (example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (349 mg, 69.2%) . The peptide (342 mg) and 0.342 mL of anisole were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (227 mg, 90%; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 10.8 to 19.8% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (22.5% recovery, overall yield 12.1%); FAB-MS: [M+H] = 589.34. Example 18 cyclo-(NMeGly-NMeArg-Gly-Asp-Mamb) ; J = NMeGly, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO:6) The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Ma b) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.43 mmol scale to give the protected cyclic peptide (205 mg, 60%) . The peptide (200 mg) and 200 μL of _n-cresol were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate (18) as a pale yellow solid (148 mg, 97%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 22% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of (18) as a fluffy white solid (14.7% recovery, overall yield 7.9%); FAB-MS: [M+H] = 547.34. Example 24 cyclo-(Pro-NMeArg-Gly-Asp-Mamb) ; J = Pro, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO:3) The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.43 mmol scale to give the protected cyclic peptide (170 mg, 48.8%). The peptide (164 mg) and 164 μL of jn-cresol were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate (24) as a pale yellow solid (101 mg, 79% ; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 22% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of (24) as a fluffy white solid (5.8% recovery, overall yield 2.1%) ;FAB-MS: [M+H] = 573.46. Example 25 cyclo-(D-Pro-NMeArg-Gly-Asp-Mamb) ; J = D-Pro, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.43 mmol scale to give the protected cyclic peptide (211mg, 60.8%). The peptide (200 mg) and 200 μL of m-cresol were treated with anhydrous hydrogen o fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate (25) as a pale yellow solid (145 mg, 93.3%; calculated as the acetate salt). Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 22% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of (25) as a fluffy white solid (6.4% recovery, overall yield 3.3%); FAB-MS: [M+H] = = 573.35. Example 28c cyclo-(β-Ala-NMeArg-Gly-Asp-Mamb) ; J = β-Ala, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO:2) The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.586 mmol scale to give the protected cyclic peptide (264 mg, 5/ ' .5%). The peptide (258 mg) and 258 μL of anisole were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound as a pale yellow solid (231 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 5.4 to 14.4% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (53.2% recovery, overall yield 32.5%); FAB-MS: [M+H] = 547.28. Example 28f cyclo-(D-Tyr-NMeArg-Gly-Asp-Mamb) ; J = D-Tyr, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.313 mmol scale to give the protected cyclic peptide (342 mg, greater than quantitative yield) . The peptide (331 mg) and 0.330 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (218 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (11.3% recovery, overall yield 10.8%); FAB-MS: [M+H] = 639.54. Example 29 cyclo-(Gly-Arg-Gly-Asp-Mamb) ; J = Gly, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO:5) The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.283 mmol scale and half was cyclized to give the protected cyclic peptide (62 mg, 58%) . The peptide (60 mg) and 60 μL of m-cresol were treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (48 mg, > quantitative yield; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.30%/ min. gradient of 0 to 9% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (36% recovery, overall yield 19.9%); FAB-MS: [M+H] = 519.26. Example 30 cyclo-(D-Ala-Arg-Gly-Asp-Mamb) ; J = D-Ala, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.189 mmol scale to give the protected cyclic peptide (211 mg, >quantitative yield) . The peptide (195 mg) and 195 μL of /n-cresol were treated with anhydrous hydrogen o fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (125 mg, 83%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 11% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (12.5% recovery, overall yield 13.8%); FAB-MS: [M+H] = 533.26. Example 31 cyclo-(Ala-Arg-Gly-Asp-Mamb) ; J = Ala, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.324 mmol scale to give the protected cyclic peptide (191 mg, 76.4%) . The peptide (100 mg) and 100 mL of /π-cresol , o were treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (75 mg, 97.4%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 11% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (15.5% recovery, overall yield 10.5%); FAB-MS: [M+H] = 533.25. Example 32 cyclo-(D-Val-Arg-Gly-Asp-Mamb) ; J = D-Val, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.193 mmol scale to give the protected cyclic peptide (199 mg, > quantitative yield) . The peptide (193 mg) and 193 μL of i7!-cresol were treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (130 g, 86%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 13% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (57% recovery, overall yield 58.1%); FAB-MS: [M+H] = 561.22. Example 33 cyclo-(D-Leu-Arg-Gly-Asp-Mamb) ; J = D-Leu, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.202 mmol scale to give the protected cyclic peptide (152 mg, 93%) . The peptide (150 mg) and 150 μL of m-cresol were o treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (78 mg, 66%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 5 to 18% acetonitrile containing 0.1% trifluoroacetic acid and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (26% recovery, overall yield 14.8%); FAB-MS: [M+H] = 575.45. Example 34 cyclo-(D-Abu-Arg-Gly-Asp-Mamb) ; J = D-Abu, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.193 mmol scale to give the protected cyclic peptide (210 mg, > quantitative yield) . The peptide (206 mg) and 206 μL of _n-cresol were treated with anhydrous hydrogen fluoride o at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (158 mg, 99%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 11% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (57% recovery, overall yield 72.2%); FAB-MS: [M+H] = 547.21. Example 35 cyclo-(D-Ser-Arg-Gly-Asp-Mamb) ; J = D-Ser, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.193 mmol scale to give the protected cyclic peptide (224 mg, > quantitative yield) . The peptide (210 mg) and 210 μl of _n-cresol were treated with anhydrous hydrogen fluoride at 0°C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (145 mg, 89%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 2 to 13% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (22% recovery, overall yield 27%); FAB-MS: [M+H] = 549.31. Example 36 cyclo-(D-Phe-Arg-Gly-Asp-Mamb) ; J = D-Phe, K = Arg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.266 mmol scale to give the protected cyclic peptide (202 mg, 90%) . The peptide (157 mg) and 157 mL of jn-cresol were treated with anhydrous hydrogen fluoride at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the title compound as a pale yellow solid (125 mg, > quantitative yield; calculated as the acetate salt) . Purification was accomlished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 23% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (35% recovery, overall yield 29.3%); FAB-MS: [M+H] = 609.25 Example 37 cyclo-(Phe-Arg-Gly-Asp-Mamb) ; J = Phe, K ~ Arg, L = Gly, M = Asp, R 1 = R 2 = H (SEQ ID NO : 4 ) The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The peptide was prepared on a 0.335 mmol scale to give the protected cyclic peptide (306 mg, > quantitative yield) . The peptide (275 mg) and 275 μL of m-cresol were treated with anhydrous hydrogen fluoride o at 0 C for 1 hour. The crude material was precipitated with ether, redissolved in aqueous .HOAc, and lyophilized to generate the title compound as a pale yellow solid (214 mg, 98%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 23% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (32% recovery, overall yield 31.5%); FAB-MS: [M+H] = 609.26 Example 40 cyclo-(D-Val-NMeAmf-Gly-Asp-Mamb) ; J = D-Val, K = NMeA f, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.586 mmol scale to give the protected cyclic peptide (189 mg, 39.9%). The peptide (189 mg) and 0.189 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (212 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 10.8 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (8.1% recovery, overall yield 4.1%); FAB-MS: [M+H] = 595.23. Example 48a The title compound may be synthesized using procedures described in Mosher et al. Tett. Lett. 29: 3183-3186, and as shown schematically below. This same procedure is a generally useful method for converting a primary amine into a guanidine functionality. Examples 42-45 The synthesis of Examples 42-45 is shown schematically below. ,SH ,S(CH2) 2 NH 2 n = 1, 2 42,44 R5 = H, CH3 see synthesis of compound 41 Examples 46 and 47 Examples 46 and 47 are prepared according to standard procedures, for example, as described in Garigipati, Tett. Lett . (1990) 31: 1969-1972 and in Canadian Patent 2008311, as is shown schematically below. The aspartic acid group may be protected (e.g., with a phenacyl protection group) to avoid side reactions . 1) H2S/Pyr/Et 3 N n = 0, 1 2} Mel/acetone 3) Amm. acetate Example 54 cyclo-(D-Val-NMeArg-β-Ala-Asp-Mamb) ; J = D-Val, K = NMeArg, L = β-Ala, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.586 mmol scale to give the protected cyclic peptide (227 mg, 46.9%) . The peptide (219 mg) and 219 μL of anisole were treated with anhydrous o hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate (54) as a pale yellow solid (150 mg, 93.2%; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7.2 to 16.2% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of (54) as a fluffy white solid (43.6% recovery, overall yield 16.5%); FAB-MS: [M+H] = 589.32. Examples 55-58 The synthesis of Examples 55-58 is shown schematically below . 1) 25% TFA in DCM 2) 10% DIEA in DCM BOC-Asp-Mamb-oxime ~ - 3) Br(CH 2 ) n COOH n = 1,2 DCC Example 58c cyclo-(D-Val-NMeArg-L-Ala-Asp-Mamb) ; J = D-Val, K = NMeArg, L = L-Ala, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (375 mg, 74.6%). The peptide (360 mg) and 0.360 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (220 mg, 83%; calculated as the fluoride salt) . Purification was accomplished by reversed- phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (19.9% recovery, overall yield 10.6%); FAB-MS: [M+H] = 589.31. Example 63 and 63a cyclo- (D-Val-NMeArg-Gly-α-MeAsp-Mamb) ; J is D-Val ; K is NMeArg; L is Gly; M is OC-MeAsp; R 1 = R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val-NMeArg-Gly-Asp- Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.794 mmol scale to give the protected cyclic peptide (237 mg, 36.1%). The peptide (237 mg) and 0.237 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (165 mg, 94.3%; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid; isomer #1 (8.36% recovery, overall yield 2.5%); FAB-MS: [M+H] = 589.29; isomer #2 (9.16% recovery, overall yield 2.7%); FAB-MS: [M+H] = 589.27. Example 64 and 64 cyclo-(D-Val-NMeArg-Gly-β-MeAsp-Mamb) ; J = D-Val, K = NMeArg, L = Gly, M = β-MeAsp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (201 mg, 40.0%). The peptide (200 mg) and 0.200 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (162 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid; isomer #1 (12.7% recovery, overall yield 4.8%); FAB-MS: [M+H] = 589.43; isomer #2 (13.9% recovery, overall yield 5.3%); FAB-MS: [M+H] = 589.45. Example 64b cyclo-(D-Val-NMeArg-Gly-NMeAsp-Mamb) ; J = D-Val, K = NMeArg, L = Gly, M = NMeAsp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (232 mg, 46.1%). The peptide (225 mg) and 0.225 mL of anisole were treated with anhydrous hydrogen o fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (160 mg, 96.4%; calculated as the fluoride salt) . Purification was accomplished by reversed- phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (28.2% recovery, overall yield 10.9%); FAB-MS: [M+H] = 589.42. Example 64c cyclo-(D-Val-NMeArg-Gly-D-Asp-Mamb) ; J = D-Val, K - NMeArg, L = Gly, M = D-Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described above for cyclo- (D-Val- NMeArg-Gly-Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.611 mmol scale to give the protected cyclic peptide (257 mg, 51.9%). The peptide (250 mg) and 0.250 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (192 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (44.4% recovery, overall yield 20.7%); FAB-MS: [M+H] = 575.42. Examples 68 and 68a cyclo-(D-Val-NMeArg-Gly-D-Asp-MeMAMB) ; J = D-Val, K = NMeArg, L = Gly, M = D-Asp, R 1 = CH3, R 2 = H MeMAMB linker was prepared via Scheme 4 (described earlier) . The title compound was made by following the solution phase synthetic route to attach MeMAMB to the tripeptide. Cyclization gave the protected cyclic peptide. Deprotection was achieved by treatment of the peptide (390 mg) and anisol (0.390 ml) with anhydrous HF at 0°C for 30 minutes. The crude material was precipitated with ether, redissolved in 10% aqueous acetic acid, and lyophilized to give a mixture of the two isomers (330 mg; greater than quantitative yield; calculated as the acetate salt) . Purification and the separation of the isomers was accomplished by Reverse- Phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.48%/min gradient of 7 to 23% acetonitrile containing 0.1% TFA. Fractions collected at Rf 24.1 min and 26.8 min were lyophilized to give the TFA salts of the isomers 1 and 2 respectively. FAB-MS (Isomer 1) : [M+H] = 589.31; FAB-MS (isomer 2) : [M+H] = 589.31. Examples 76 and 76a cyclo-(D-Val-NMeArg-Gly-D-Asp-PhMAMB) ; J = D-Val, K = NMeArg, L = Gly, M = D-Asp, R 1 = Ph, R 2 = H PhMAMB linker was prepared via Scheme 4 (described earlier) . The title compound was made by following the solution phase synthetic route to attach PhMAMB to the tripeptide. Cyclization gave the protected cyclic peptide. Deprotection was achieved by treatment of the peptide (470 mg) and anisol (0.470 ml) with anhydrous HF at 0°C for 30 minutes. The crude material was precipitated with ether, redissolved in 10% aqueous acetic acid, and lyophilized to give a mixture of the two isomers (310 mg; 82.4% overall recovery). Purification and the separation of the isomers was accomplished by Reverse-Phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.55%/min gradient of 18 to 36% acetonitrile containing 0.1% TFA. Fractions collected at Rf 22 min and 24.6 min were lyophilized to give the TFA salts of the isomers 1 and 2 respectively. FAB-MS (Isomer 1): [M+H] = 651.33; FAB-MS (isomer 2): [M+H] = 651.33. Example 79 cyclo-(D-Val-NMeArg-Gly-Asp-NMeMamb) ; J = D-Val, K = NMeArg, L = Gly, M = Asp, R 1 = H, R 2 = CH 3 The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-NMeMamb to the oxime resin. The peptide was prepared on a 0.456 mmol scale to give the protected cyclic peptide (406 mg, greater than quantitative yield) . The peptide (364 mg) and 0.364 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (251 mg, 93.5%; calculated as the fluoride salt). Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 9 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (34.2% recovery, overall yield 29.9%); FAB-MS: [M+H] = 589.33. Example 87,88 cyclo-(D-Val-NMeArg-Gly-Asp-4-aminomethylbenzoic acid); The title compound was prepared using the general procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The DCC/DMAP method was used for attachment of Boc-4-aminomethylbenzoic acid to the oxime resin. The peptide was prepared on a 0.43 mmol scale to give the protected cyclic peptide (212mg, 60.8%). The peptide (200 mg) and 200 μL of m-cresol were treated o with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous HOAc, and lyophilized to generate the crude peptide as a pale yellow solid (152 mg, 97% ; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 7 to 22% acetonitrile containing 0.1% TFA. Two peaks were isolated to give isomer #1 (87) (17.1% recovery, overall yield 9.3%) and isomer #2 (88) (13.4% recovery, overall yield 7.3%); FAB-MS: [M+H] = 575.41 (isomer #1; 87); 575.44 (isomer #2; 88) . Example 89a and 89b cyclo-(D-Val-NMeArg-Gly-Asp-aminotetralincarboxylic acid) ; J = D-Val, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc- aminotetralin-carboxylic acid to the oxime resin. The peptide was prepared on a 0.164 mmol scale to give the protected cyclic peptide (69 mg, 49.3%) . The peptide (69 mg) and 0.069 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (59.7 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 16.2 to 27% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid. Two isomers were obtained; isomer #1 (12.5% recovery, overall yield 6.2%, FAB-MS: [M+H] = 615.34; isomer #2 (18.6% recovery, overall yield 9.3%, FAB-MS: [M+H] = 615.35. Example 89c cyclo-(D-Val-NMeArg-Gly-Asp-aminomethylnaphthoic acid); J = D-Val, K = NMeArg,L = Gly, M = Asp, R 1 = H, R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Ma b) (Example 4) . The DCC/DMAP method was used for attachment of Boc-aminomethyl- naphthoic acid to the oxime resin. The peptide was prepared on a 0.737 mmol scale to give the protected cyclic peptide (463 mg, 73.1%). The peptide (463 mg) and 0.463 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 20 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (349 mg, greater than quantitative yield; calculated as the fluoride salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.45%/ min. gradient of 4.5 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (12.1% recovery, overall yield 7.8%); FAB-MS: [M+H] = 625.32. Example 89d cyclo-(D-Abu-NMeArg-Gly-Asp-iodo-Mamb) ; J = D-Abu, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H, R 10 = I The title compound was prepared using the general procedure described above for cyclo- (D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-iodo-Mamb to the oxime resin. The peptide was prepared on a 3.53 mmol scale to give the protected cyclic peptide (4.07 g, greater than quantitative yield) . The per.tide (4.07 g) and 4.0 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes . The crude material was precipitated with ether, redissolved in aqueous acetic acid, and lyophilized to generate the title compound (2.97 g, greater than quantitative yield; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.16%/ min. gradient of 16.2 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (28.7% recovery, overall yield 30.2%); FAB-MS: [M+H] = 687.33. Example 89e cyclo-(D-Abu-di-NMeOrn-Gly-Asp-Mamb) ; J = D-Abu, K = di-NMeOrn, L = Gly, M = Asp, R 1 = R 2 = H The title compound was prepared using the general procedure described for cyclo-(D-Val- NMeArg-Gly-Asp-Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-Mamb to the oxime resin. The peptide was prepared on a 0.498 mmol scale to give the protected cyclic peptide (150 mg, 39.3%). The peptide (150 mg) and 0.150 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes. The crude material was precipitated with ether, redissolved in aqueous acetonitrile, and lyophilized to generate the title compound (93 mg, 86%; calculated as the fluoride salt) . Purification was accomplished by reversed- phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.45%/ min. gradient of 3.6 to 18% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA salt of the title compound as a fluffy white solid (49.3% recovery, overall yield 14.2%); FAB-MS: [M+H] = 533.34. Example 90 cyclo- .D-Val-NMeArσ-Gly-Asp-2-aminomethylphenylacetic acid) The title compound was prepare by a modification of the general solution-phase chemistry route . This approach employed an amino acid succinimide ester coupling to the aromatic linker, and the dmitrobenzophenone oxime as shown schematically below in the Scheme below (n = 1) . Scheme Boc-As .OcHex)-2-aminomethylphenylace ic Acid To a suspension of 2-aminomethylphenylacetic acid«HCl (4.0 g, 20 mmol) in H2O (20 ml) was added NaHCOβ (5.0 g, 60 116 SUBSTITUTE SHEET mmol), followed by a solution of Boc-Asp(OcHex)-OSu (7.5 g, 18 mmol) in THF (20 ml) . The reaction mixture was stirred at room temperature for 3 hours, filtered, diluted with H2θ, acidified with IN HCl, and extracted with ethyl acetate. The extracts were washed with H2O, brine, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. This material was triturated with ether to provide the title compound (7.0 g, 83%) as a white powder. ^H NMR (D6-DMS0) 12.40 (br s, IH) , 8.30 (br t, IH) , 7.20 (m, 5H) , 4.65 (m, IH) , 4.35 (q, IH) , 4.25 (m, 2H) , 3.65 (s, 2H) , 2.70 (dd, IH), 2.55 (dd, IH) , 1.70 (m, 4H) , 1.40 (s, 9H) , 1.35 (m, 6H) . 4.4 '-Dinitrobenzophenone Oxime The title compound was prepared by modification of procedures previously reported in the literature (Chapman and Fidler (1936) J. Chem . Soc, 448; Kulin and Leffek (1973) Can . J. Chem. , 51: 687) . A solution of chromic anhydride (20 g, 200 mmol) in 125 ml of H2O was added dropwise over 4 hours, to a suspension of bis (4-nitrophenyl)methane (25 g, 97 mmol) in 300 ml of acetic acid heated to reflux. The reaction mixture was heated at reflux for 1 hour, cooled to room temperature, and poured into water. The solid was collected by filtration, washed with H2O, 5% sodium bicarbonate, H2O, and air-dryed to provide a 1:1 mixture of bis (4- nitrophenyl)methane/4, 4 '-dmitrobenzophenone via ^H NMR. This material was oxidized with a second portion of chromic anhydride (20 g, 200 mmol) , followed by an identical work-up procedure to provide the crude product . Trituration with 200 ml of benzene heated to reflux for 16 hours provided 4,4'- dinitrobenzophenone (20.8 g, 79%) as a yellow powder. A solution of hydroxylamine hydrochloride (10.2 g, 147 mmol) was added to a suspension of 4, '-dmitrobenzophenone (19 g, 70 mmol) in 100 ml of ethanol. The reaction mixture was heated to reflux for 2 hours, cooled to room temperature, 117 SUBSTITUTESHEET and the solid collected by filtration. Recrystallization from ethanol provided the title compound (14.0 g, 70%) as pale yellow crystals, mp 194°C; λ R NMR (D6-DMS0) 12.25 (s, IH) , 8.35 (d, 2H) , 8.20 (d, 2H) , 7.60 (d, 4H) . 4.4 , -Dinit obβnzoρhf.nnne Oxime Boc-Asp (OcHex) -2- aminomet--ylP--enylacetate To an ice-cooled solution of Boc-Asp(OcHex)-2- aminomethylphenylacetic acid (3.5 g, 7.6 mmol) and 4,4'- dinitrobenzophenone oxime (2.2 g, 7.5 mmol) in 50 ml of ethyl acetate and 5 ml of DMF was added DCC (1.6 g, 7.8 mmol) . The reaction mixture was stirred at room temperature for 8 hours, filtered, diluted with ethyl acetate, washed with saturated sodium bicarbonate solution, H2O, brine, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. This material was purified by column chromatography on silica gel (EM Science, 230-400 mesh) using 10:1 dichloromethane/ethyl acetate to give the title compound (4.3 g, 78%) as pale yellow crystals. NMR (Dβ-DMSO) 8.30 (dd, 5H), 7.80 (d, 2H), 7.65 (d, 2H) , 7.15 (m, 5H) , 4.65 (m, IH) , 4.35 (q, IH) , 4.15 (m, 2H) , 3.90 (s, 2H) , 2.70 (dd, IH) , 2.50 (dd, IH) , 1.70 (m, 4H) , 1.40 (s, 9H) , 1.35 (m, 6H) . 4.4 '-Dinitrobenzophenone Oxime Boc-D-Val-NMeArσ.Tos) -Gly- Asp (OcHex)-2-aminom thylphenylacetate To a solution of 4, '-dinitrobenzophenone oxime Boc- Asp(OcHex)-2-aminomethylphenylacetate (1.5 g, 2 mmol) in 4 ml of dichloromethane was added 2 ml of trifluoroacetic acid. The reaction mixture was stirred at room temperature for 1 hour, diluted with dichloromethane, and evaporated to dryness under reduced pressure. The oily residue was concentrated under high vacuum to remove traces of excess trifluoroacetic acid. To a solution of the crude TFA salt and Boc-D-Val- NMeArg(Tos)-Gly (1.2 g, 2 mmol) in 5 ml of DMF was added TBTU 118 (640 mg, 2 mmol) and DIEA (780 mg, 6 mmol) . The reaction mixture was stirred at room temperature for 16 hours, concentrated under high vacuum, diluted with ethyl acetate, washed with 5% citric acid, H2O, brine, dried over anhydrous magnesium sulfate, and evaporated to dryness under reduced pressure. This material was triturated with ether to provide the title compound (2.3 g, 95%) as a yellow powder. This material was used without further purification. cyclo- .D-V l-NMeArσ .Tos) -Gly-Aao .OcHex) -2- aminomethylphenylacetic acid) To a solution of 4, 4 '-dinitrobenzophenone oxime Boc-D- Val-NMeArg(Tos)-Gly-Asp(OcHex)-2-aminomethylphenylacetate (1.2 g, 1 mmol) in 4 ml of dichloromethane was added 2 ml of trifluoroacetic acid. The reaction mixture was stirred at room temperature for 3 hours, diluted with dichloromethane, and evaporated to dryness under reduced pressure. The oily residue was concentrated under high vacuum to remove traces of excess trifluoroacetic acid. To a solution of the crude TFA salt in 100 ml of DMF was added acetic acid (0.50 ml, 8.7 mmol) and DIEA (1.52 ml, 8.7 mmol) . The reaction mixture was stirred at 60°C for 3 days, concentrated under high vacuum, diluted with ethyl acetate, and the solution allowed to crystallize overnight . Filtration provided the title compound (563 mg, 68%) as a yellow powder. 1 H NMR (D6-DMSO) 8.70 (d, IH) , 8.40 (br s, IH) , 8.30 (br s, IH) , 8.05 (t, IH), 7.65 (d, 2H) , 7.25 (d, 2H) , 7.20 (m, 4H) , 7.10 (br d, IH) , 6.80 (br s, IH) , 6.60 (br s, IH) , 5.10 (dd, IH) , 4.65 (m, IH) , 4.55 (m, IH) , 4.40 (m, 2H) , 3.85 (m, 2H) , 3.65 (d, IH) , 3.45 (m, 2H) , 3.05 (m, 2H) , 2.80 (s, 3H) , 2.80 (m, IH) , 2.60 (dd, IH) , 2.30 (s, 3H) , 1.70 (m, 6H) , 1.30 (m, 9H) , 0.95 (d, 3H), 0.80 (d, 3H) ; DCI(NH3)-MS: [M+H] = 825. cyclo- .n-Val-NMeArσ-Gly-Asp-2-aminomethylphenylacetiπ aci ) 119 SUBSTITUTESHEET A mixture of 352 mg (0.43 mmol) of cyclo-(D-Val- NMeArg(Tos)-Gly-Asp(OcHex)-2-aminomethylphenylacetic acid) and 352 μl of anisole was treated at 0°C with 5 ml of HF for 20 minutes. The excess HF was removed under reduced pressure, the residue triturated with ether, dissolved in 50% acetonitrile/H2θ, and lyophilized to provide the crude cyclic peptide»HF salt as an off-white powder. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (225 mg, 75%) as a fluffy white solid; X H NMR (D6-DMSO) 8.70 (d, IH) , 8.35 (d, IH) , 8.20 (t, IH), 8.00 (t, IH) , 7.45 (t, IH) , 7.20 (m, 3H) , 7.10 ( , IH), 7.00 (br s, 4H) , 5.10 (dd, IH) , 4.50 (dt, IH) , 4.40 (m, 2H), 3.85 (dt, 2H) , 3.65 (d, IH) , 3.50 (dd, IH) , 3.45 (d, IH) , 3.10 ( , 2H), 2.90 (s, 3H) , 2.75 (dd, IH) , 2.55 (dd, IH) , 2.00 (m, IH) , 1.85 ( , IH) , 1.65 (m, IH) , 1.30 (m, 2H) , 0.95 (d, 3H) , 0.85 (d, 3H) ; FAB-MS: [M+H] = 589. Example 91 cyclo- (D-Val-NMeArσ-Gly-Asp-2-aminoιrtethylbenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-2-aminomethylphenylacetic acid) , and as shown schematically above in the Example 90 Scheme (n = 0) . The cyclic peptide (192 mg, 0.24 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (20 mg, 12%) as a fluffy white solid; ^H NMR (Dς- DMSO) 8.75 (d, IH) , 8.50 (d, IH) , 7.65 (t, IH) , 7.60 (t, IH) , 7.50 (m, 2H) , 7.40 ( , 3H) , 7.00 (br s, 4H) , 5.05 (dd, IH) , 4.50 (t, IH), 4.30 (m, 2H) , 4.10 (dd, IH) , 3.70 (m, 2H) , 3.15 120 SUBSTITUTESHEET (q, 2H) , 3.05 (s, 3H) , 2.80 (dd, IH) , 2.55 (dd, IH) , 2.10 (m, IH) , 1.95 (m, IH) , 1.60 (m, IH) , 1.40 (m, 2H) , 1.05 (d, 3H) , 0.95 (d, 3H) ; FAB-MS: [M+H] = 575. Example 92 cyclo- .D-V l-NMeArσ-Glγ-Asp-3-aminophenylacetic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) , and as shown schematically in the Scheme below. The cyclic peptide (360 mg, 0.44 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative LiChrospher RP-18 column (5 cm) using a 2.3% / minute gradient of 22 to 90% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (150 mg, 50%) as a fluffy white solid; 1 H NMR (Dβ- DMSO) 12.40 (br s, IH) , 8.95 (s, IH) , 8.55 (m, 2H) , 8.45 (t, IH), 7.90 (d, IH), 7.50 (m, IH) , 7.20 (t, IH) , 7.00 (br s, 4H) , 6.90 (m, 2H) , 5.15 (dd, IH) , 4.65 (q, IH) , 4.55 (t, IH) , 3.65 (m, 2H) , 3.60 (dd, IH) , 3.10 (m, 2H) , 2.85 (s, 3H) , 2.85 (d, IH), 2.70 (dd, 2H) , 2.00 (m, 2H) , 1.75 (m, IH) , 1.35 (m, 2H) , 0.90 (d, 3H) , 0.85 (d, 3H) ; FAB-MS: [M+H] = 575. 121 SUBSTITUTESHEET Scheme H-Ox, DCC, DMAP, EtOAc Example 93 cyclo- (D-Val-NMeArσ-Gly-Asp-3-aminomethvl-4-chlorobenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) . The cyclic peptide (240 mg, 0.28 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative LiChrospher RP-18 column (5 cm) using a 1.4% / minute gradient of 22 to 90% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title 122 SUBSTITUTESHEET compound (80 mg, 39%) as a fluffy white solid; 1 H NMR (DQ- DMSO) 9.00 (d, IH) , 8.50 (d, IH) , 8.45 (t, IH) , 7.60 (d, 2H) , 7.45 (s, IH), 7.45 (d, 2H) , 7.00 (br s, 4H) , 5.15 (dd, IH) , 4.45 (m, 2H), 4.20 (m, 2H) , 4.10 (d, IH) , 3.55 (d, IH) , 3.10 (m, 2H), 2.90 (s, 3H) , 2.65 (dd, IH) , 2.50 ( , IH) , 2.05 (m, 2H) , 1.50 (m, IH), 1.30 (m, 2H) , 1.05 (d, 3H) , 0.85 (d, 3H) ; FAB-MS: [M+H] = 609. Example 9 cyclo- (D-Val-NMeArg-Gly-Asp-iodo-Mamb) ; J = D-Val, K = NMeArg, L = Gly, M = Asp, R 1 = R 2 = H, R 10 = I The title compound was prepared using the general procedure described for cyclo- (D-Val-NMeArg-Gly-Asp- Mamb) (Example 4) . The DCC/DMAP method was used for attachment of Boc-iodo-Mamb to the oxime resin. The peptide was prepared on a 1.05 mmol scale to give the protected cyclic peptide (460 mg, 46.8%) . The peptide (438 mg) and 0.5 mL of anisole were treated with anhydrous hydrogen fluoride at 0 C for 30 minutes . The crude material was precipitated with ether, redissolved in aqueous acetic acid, and lyophilized to generate the title compound (340 mg, 95.6%; calculated as the acetate salt) . Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.23%/ min. gradient of 12.6 to 22.5% acetonitrile containing 0.1% TFA and then lyophilized to give the TFA 123 SUBSTITUTESHEET salt of the title compound as a fluffy white solid (39.7% recovery, overall yield 16.6%); FAB-MS: [M+H] = 701.37. Example 95 cyclo- .D-Val-NMeArσ-Gly-Asp-3-aminomethyl-4-methoxybenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) . The cyclic peptide (600 mg, 0.71 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.33% / minute gradient of 7 to 18% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (104 mg, 32%) as a fluffy white solid; 1 H NMR (Dβ- DMSO) 12.40 (br s, IH) , 8.25 (d, IH) , 8.20 (br s, IH) , 8.00 (br s, 2H), 7.85 (d, IH) , 7.75 (s, IH) , 7.65 (br s, IH) , 7.05 (d. IH), 7.05 (br s, 4H) , 5.00 (dd, IH) , 4.60 (q, IH) , 4.30 (d, IH), 4.25 (d, 2H) , 3.85 (s, 3H) , 3.85 (dd, IH) , 3.70 (dd, IH) , 3.10 (q, 2H) , 3.00 (s, 3H) , 2.70 (m, IH) , 2.50 (m, IH) , 2.10 (m, IH) , 1.90 (m, IH) , 1.65 (m, IH) , 1.35 (m, 2H) , 1.00 (d, 3H), 0.90 (d, 3H) ; FAB-MS: [M+H20+H] = 623. Example 96 cvclo-fD-Val-NMeArσ-Glγ-Asp-3-aminomethyl-4-methylhen7.o.r. acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) . The cyclic peptide (210 mg, 0.25 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative LiChrospher RP-18 column (5 cm) using a 2.3% / minute gradient of 22 to 90% acetonitrile containing 124 SUBSTITUTESHEET 0.1% trifluoroacetic acid to give the TFA salt of the title compound (75 mg, 42%) as a fluffy white solid; 1 H NMR (Dβ- DMSO) 12.30 (br s, IH) , 8.85 (d, IH) , 8.55 (d, IH) , 8.30 (t, IH), 7.75 (d, IH), 7.55 (m, 2H) , 7.40 (s, IH) , 7.20 (s, IH) , 7.00 (br s, 4H) , 5.20 (dd, IH) , 4.55 (q, IH) , 4.45 (dd, IH) , 4.30 (m, 2H), 4.05 (dd, IH) , 3.60 (d, IH) , 3.10 (q, 2H) , 3.00 (s, 3H), 2.70 (dd, IH), 2.50 ( , IH) , 2.25 (s, 3H) , 2.10 (m, 2H), 1.60 (m, IH), 1.35 (m, 2H) , 1.10 (d, 3H) , 0.90 (d, 3H) ; FAB-MS: [M+H] = 589. Example 97 cyclo- .D-Val-NMeArσ-Gly-Asp-3-aminomethyl-6-chloroben..oio acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) , except that 4, 4 '-dinitrobenzophenone oxime was employed. The cyclic peptide (550 mg, 0.65 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (254 mg, 54%) as a fluffy white solid; 1 H NMR (Dβ- DMSO) 12.30 (br s, IH) , 9.05 (d, IH) , 8.45 (m, 2H) , 7.50 (t, IH) , 7.35 (d, IH) , 7.30 (m, 2H) , 7.10 (s, IH) , 7.05 (br s, 4H) , 5.15 (dd, IH) , 4.45 (dd, IH) , 4.40 (q, 2H) , 4.05 (dt, 2H) , 3.55 (dd, IH) , 3.15 (q, 2H) , 3.10 (s, 3H) , 2.70 (dd, IH) , 2.50 (m, IH), 2.05 (m, 2H) , 1.65 (m, IH) , 1.35 (m, 2H) , 1.10 (d, 3H) , 0.90 (d, 3H) ; FAB-MS: [M+H] = 609. Example 98 cyclo- .D-Val-NMeArσ-Gly-Asp-3-aminomethyl-6-iodobenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- 125 SUBSTITUTESHEET Asp-Mamb), except that 4, 4 '-dinitrobenzophenone oxime was employed. The cyclic peptide (490 mg, 0.52 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (194 mg, 46%) as a fluffy white solid; ^ NMR (D6~ DMSO) 12.30 (br s, IH) , 9.00 (d, IH) , 8.40 ( , 2H) , 7.70 (d, IH) , 7.50 (m, IH) , 7.30 (m, IH) , 7.05 (d, IH) , 7.00 (s, IH) , 7.00 (br s, 4H), 5.15 (dd, IH) , 4.40 (d, IH) , 4.40 (q, 2H) , 4.0 ( , 2H), 3.55 (dd, IH) , 3.15 (q, 2H) , 3.10 (s, 3H) , 2.70 (dd, IH), 2.50 (m, IH) , 2.05 (m, 2H) , 1.65 (m, IH) , 1.35 (m, 2H) , 1.15 (d, 3H), 0.90 (d, 3H) ; FAB-MS: [M+H] = 701. Example 99 cyclo- .D-Val-NMeΑrσ-Glγ-Αsp-3-aminomethyl-6-methoxybenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo- (D-Val-NMeArg-Gly- Asp-Mamb) , except that 4, 4 '-dinitrobenzophenone oxime was employed. The cyclic peptide (256 mg, 0.30 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (137 mg, 63%) as a fluffy white solid; 1 H NMR (D6~ DMSO) 8.45 (d, IH) , 8.40 (d, IH) , 8.30 (t, IH) , 7.65 (d, IH) , 7.50 (t, IH) , 7.40 (s, IH) , 7.35 (d, IH) , 7.05 (d, IH) , 7.00 (br s, 4H), 5.20 (dd, IH) , 4.55 (dd, IH) , 4.50 (q, IH) , 4.35 (dd, IH), 4.25 (dd, IH) , 3.95 (dd, IH) , 3.90 (s, 3H) , 3.55 (d, IH), 3.10 (q, 2H) , 3.00 (s, 3H) , 2.70 (dd, IH) , 2.50 (m, IH) , 2.05 (m, 2H) , 1.60 ( , IH) , 1.35 ( , 2H) , 1.10 (d, 3H) , 0.95 (d, 3H) ; FAB-MS: [M+H] = 605. 126 SUBSTITUTESHEET Example 1QQ cyclo- .D-Val-NMeΑrσ-GI γ-Asp-3-ami nomethyl-6-methγlhenzoic acid) The title compound was prepare by the general solution- phase procedure described above for cyclo-(D-Val-NMeArg-Gly- Asp-Mamb) , except that 4,4 '-dinitrobenzophenone oxime was employed. The cyclic peptide (230 mg, 0.28 mmol) was deprotected with excess HF in the presence of anisole as scavenger. Purification was accomplished by reversed-phase HPLC on a preparative Vydac C18 column (2.5 cm) using a 0.8% / minute gradient of 10 to 38% acetonitrile containing 0.1% trifluoroacetic acid to give the TFA salt of the title compound (54 mg, 27%) as a fluffy white solid; 1 H NMR (D6~ DMSO) 12.30 (br s, IH) , 8.80 (d, IH) , 8.40 (d, IH) , 8.30 (t, IH) , 7.45 (m, 2H) , 7.15 (q, 2H) , 7.00 (s, IH) , 7.00 (br s, 4H) , 5.15 (dd, IH) , 4.45 (m, 3H) , 4.05 (m, 2H) , 3.55 (dd, IH) , 3.10 (q, 2H), 3.05 (s, 3H) , 2.70 (dd, IH) , 2.50 (m, IH) , 2.30 (s, 3H) , 2.05 (m, 2H) , 1.60 (m, IH) , 1.35 (m, 2H) , 1.05 (d, 3H), 0.90 (d, 3H) ; FAB-MS: [M+H] = 589. 127 SUBSTITUTESHEET Utility The compounds of this invention possess antiplatelet efficacy, as evidenced by their activity in standard platelet aggregation assays or platelet fibrinogen binding assays, as described below. A compound is considered to be active in these assays if it has an IC50 value of less than about 1 mM. Platelet aggregation and fibrinogen binding assays which may used to demonstrate the antiplatelet activity of the compounds of the invention are described below. Platelet Aggregation Assay: Venous blood was obtained from the arm of a healthy human donor who was drug-free and aspirin-free for at least two weeks prior to blood collection. Blood was collected into 10 ml citrated Vacutainer tubes. The blood was centrifuged for 15 minutes at 150 x g at room temperature, and platelet-rich plasma (PRP) was removed. The remaining blood was centrifuged for 15 minutes at 1500 x g at room temperature, and platelet-poor plasma (PPP) was removed. Samples were assayed on a aggregometer (PAP-4 Platelet Aggregation Profiler) , using PPP as the blank (100% transmittance) . 200 μl of PRP was added to each micro test tube, and transmittance was set to 0%. 20 μl of various agonists (ADP, collagen, arachidonate, epinephrine, thrombin) were added to each tube, and the aggregation profiles were plotted (% transmittance versus time) . The results were expressed as % inhibition of agonist-induced platelet aggregation. For the IC50 evaluation, the test compounds were added at various concentrations prior to the activation of the platelets. Platele -Fibrinoσen Binding Assay: Binding of 12 5ι- fibrinogen to platelets was performed as described by Bennett et al. (1983) Proc. Natl. Acad. Sci. USA 80: 2417-2422, with 128 SUBSTITUTESHEET some modifications as described below. Human PRP (h-PRP) was applied to a Sepharose column for the purification of platelet fractions. Aliquots of platelets (5 X 10^ cells) along with 1 mM calcium chloride were added to removable 96 well plates prior to the activation of the human gel purified platelets (h-GPP) . Activation of the human gel purified platelets was achieved using ADP, collagen, arachidonate, epinephrine, and/or thrombin in the presence of the ligand, 125 _ ibrinogen. The 1 5ι_fibrinogen bound to the activated, platelets was separated from the free form by centrifugation and then counted on a gamma counter. For an IC50 evaluation, the test compounds were added at various concentrations prior to the activation of the platelets. Dosaσe and Formulation The compounds of this invention can be administered by any means that produces contact of the active agent with the agent's site of action, glycoprotein Ilb/IIIa (GPIIb/IIIa), in the body of a mammal. They can be administered by any conventional means available for use in conjunction with pharmaceuticals, either as individual therapeutic agents or in a combination of therapeutic agents, such as a second antiplatelet agent such as aspirin or ticlopidine which are agonist-specific. They can be administered alone, but generally administered with a pharmaceutical carrier selected on the basis of the chosen route of administration and standard pharmaceutical practice. The dosage administered will, of course, vary depending upon known factors, such as the pharmacodynamic characteristics of the particular agent and its mode and route of administration; the age, health and weight of the recipient; the nature and extent of the symptoms; the kind of concurrent treatment; the frequency of treatment; and the effect desired. A daily dosage of active ingredient can be 129 SUBSTITUTESHEET expected to be about 0.01 to 10 milligrams per kilogram of body weight. Dosage forms (compositions suitable for administration contain from about 1 milligram to about 100 milligrams of active ingredient per unit. In these pharmaceutical compositions the active ingredient will ordinarily be present in an amount of about 0.5-95% by weight based on the total weight of the composition. The active ingredient can be administered orally in solid dosage forms, such as capsules, tablets, and powders, or in liquid dosage forms, such as elixirs, syrups, and suspensions. It can also be administered parenterally, in sterile liquid dosage forms . Gelatin capsules contain the active ingredient and powdered carriers, such as lactose, starch, cellulose derivatives, magnesium stearate, stearic acid, and the like. Similar diluents can be used to make compressed tablets . Both tablets and capsules can be manufactured as sustained release products to provide for continuous release of medication over a period of hours. Compressed tablets can be sugar coated or film coated to mask any unpleasant taste and protect the tablet from the atmosphere, or enteric coated for selective disintegration in the gastrointestinal tract. Liquid dosage forms for oral administration can contain coloring and flavoring to increase patient acceptance. In general, water, a suitable oil, saline, aqueous dextrose (glucose) , and related sugar solutions and glycols such as propylene glycol or polyethylene glycols are suitable carriers for parenteral solutions. Solutions for parenteral administration preferably contain a water soluble salt of the active ingredient, suitable stabilizing agents, and if necessary, buffer substances. Antioxidizing agents such as sodium bisulfite, sodium sulfite, or ascorbic acid, either alone or combined, are suitable stabilizing agents . Also used are citric acid and its salts and sodium EDTA. In addition, parenteral solutions can contain preservatives, 130 SUBSTITUTESHEET such as benzalkonium chloride, methyl- or propyl-paraben, and chlorobutanol. Suitable pharmaceutical carriers are described in Remington's Pharmaceutical Sciences. Mack Publishing Company, a standard reference text in this field. Useful pharmaceutical dosage-forms for administration of the compounds of this invention can be illustrated as follows: Capsules A large number of unit capsules are prepared by filling standard two-piece hard gelatin capsules each with 100 milligrams of powdered active ingredient, 150 milligrams of lactose, 50 milligrams of cellulose, and 6 milligrams magnesium stearate. Soft Gelatin Capsules A mixture of active ingredient in a digestable oil such as soybean oil, cottonseed oil or olive oil is prepared and injected by means of a positive displacement pump into gelatin to form soft gelatin capsules containing 100 milligrams of the active ingredient. The capsules are washed and dried. Tablets A large number of tablets are prepared by conventional procedures so that the dosage unit was 100 milligrams of active ingredient, 0.2 milligrams of colloidal silicon dioxide, 5 milligrams of magnesium stearate, 275 milligrams of microcrystallme cellulose, 11 milligrams of starch and 98.8 milligrams of lactose. Appropriate coatings may be applied to increase palatability or delay absorption. The Tables below set forth representative compounds of the present invention. 131 SUBSTITUTESHEET Table 1 The optical isomer of J is indicated. R10=H unless otherwise indicated. 132 UB TIT 133 SUBSTITUTE SHEET cyclopentyl (D) cyclopentyl ( ) cyclohexyl (D) cyclohexyl (L) cyclohexylmethyl (D) cyclohexylmethyl (L) CH(CH 3 )2 R 10 =I 701.37 (D) 134 3d H H k H H H O H H o CH 3 1 II I I II I (CH 2 ) 4 — N — C— C— N— C-O-C-CH 3 I I H CH 3 1 H H H O H H I II I I — (CH 2 ) 4 — N — C— C— N— H I H 135 SUBSTITUTE SHEET 136 SUBSTITUTE SHEET Table ] (continued) Gly / N NMeArg Asp / \ Exampl FAB-MS fM+.q. QP i l Isomer 6 - m 2^ 7 "& 137 SUBSTITUTE SHEET Table 1 Example FAB-MS fM+S . Optical No . Isomer -NHCH2CH2C (=0) - 547 .28 28c Example R3 R4 R5 FAB-MS Optical Number (M+S. Isomer 138 SUBSTITUTE SHEET Table 2 The optical isomer of J is indicated, 139 SUBSTITUTESHEET Table 3 The optical isomer of K is indicated. FAB-MS Optical (M+H) Isomer 140 SUBST Table 3 .continued) -CH2SCH2CH2NH2 (L) -CH2SCH2CH2NH2 (D) -CH2SCH2CH2NHC (=NH) (NH2) (L) -CH2SCH2CH2NHC (=NH) (NH2) (D) -CH2CH2SCH2CH2NH2 (L) -CH2CH2SCH2CH2NH2 (D) -CH2CH2SCH2CH2NHC (=NH) (NH2) (L) -CH2CH2SCH2CH2NHC(=NH) (NH2) (D) r * m (D) a CH3 ^-^ ^T ( ) CH3 ~ - C C H H2 2 --( V r-- CCH 2 NH 2 (D) b CH3 — _ CCHH 2 - Λ-/ V r C<H 2 NH 2 141 SUBSTITUTE SHEET j H 2 .NH (L) 49 CH 3 -CH 2 CH . NH ■ O- -i NH 2 NH (D) 49a CH3 -CH 2 - -CH 2 NH-( NH Example Number FAR-MS (M+H) 142 TE SHEET Table 4 NMeArg p / \ Optical Isomer 8c -NHCH(CH3)C(=0)- 589.31 (L) 143 SUBSTITUTE SHEET Table 5 144 SUBSTITUTE SHEET Table 6 The optical isomer of -CH(R 1 )N(R 2 )- is indicated. Optical Isomer isomer 1 isomer 2 R S R S R S R S R S R S R S 145 SUBSTITUTESH 146 TITUTE SHEET Table 7 Example Structure FAB-MS Ntt-i-ber (M+H) isomer 1 isomer 2 147 SUBSTITUTE SHEET Sf-rn <-.+ ι_ re T-aR-M.q ΓM+HI .yaτπ 1 e No , Gly-. Asp 687.33 89d NMeArg . I I 533.34 89e 148 SUBSTITUTE SHEET 149 SUBSTITUTE SHEET Table 10 K = - N(R 6 )CH(R 7 )C(=0) J = D-Val Example ^6 R' Qpt, Nnrober Isomer 105 CH3 -(CH 2 ) 4 ■ -—G ( NH -150- SUBSTITUTE SHEET -151- SUBSTITUTE SHEET 126 CH3 D -152- SUBSTITUTE SHEET -CH2-S-(CH2)3-NH-CH2CH 3 D -CH2-S-(CH2) 3-NH-CH (CH3) 2 -CH2-S-(CH2) 3-NH-CH (CH3) 2 D -CH2-S-(CH2)3-NH-CH2CH2~ L CH 3 134 CH3 -CH2-S-(CH2)3-NH-CH2CH2- D CH3 -CH 2 -S-(CH 2 )3-NH-C(CH3)3 L -CH2-S- ( CH2 ) 3"NH-C ( CH3 ) 3 D CH2-0- (CH2) 3-NH-CH3 L CH2-O- (CH2) 3-NH-CH3 D CH2-0-(CH2)3-NH-CH2CH3 L CH2-0- (CH2) 3-NH-CH2CH3 D CH2-0-(CH2)3-NH-CH(CH3)2 L CH2~0-(CH2) 3-NH-CH(CH3) 2 D CH2-0- (CH2) 3-NH-CH2CH2CH3 L CH2-O- (CH2) 3-NH-CH 2 CH2CH3 D CH2-0-(CH 2 )3-NH-C(CH 3 )3 L CH2-0-(CH2)3-NH-C(CH 3 ) 3 D -CH2-S-(CH2)2~NH-CH3 L -CH2-S- (CH2) 2-NH-CH3 D -CH2-S-(CH2)2-NH-CH2CH 3 L -CH2-S-(CH2)2-NH-CH2CH 3 D -CH2-S-(CH 2 )2-NH-CH(CH 3 )2 L -CH2-S-(CH2)2-NH-CH(CH3)2 D -CH2-S-(CH2)2-NH-CH2CH2- L CH3 -153- SUBSTITUTESHEET -154- SUBSTITUTE SHEET CH2~0-(CH2)4-NH-CH3 D CH2-0- (CH2) 4-NH-CH2CH3 L CH2-0-(CH2)4-NH-CH2CH3 D CH2-0-(CH2) 4-NH-CH(CH3)2 L CH2-0- ( CH2) 4-NH-CH ( CH3) 2 D CH2-0-(CH2)4-NH-CH 2 CH2CH3 L CH2-0- (CH2) 4-NH-CH 2 CH2CH3 D CH2-0- (CH2) 4-NH-C (CH3) 3 L CH2-0-(CH2) -NH-C (CH3) 3 D -CH2-S-(CH2) 5-NH-CH3 L -CH2-S-(CH2)5-NH-CH3 D -CH2-S- (CH2) 5-NH-CH2CH 3 L -CH2-S-(CH2)5-NH-CH2CH 3 D -CH2-S- ( CH2) 5-NH-CH ( CH3) 2 L -CH2~S-(CH2) 5-NH-CH ( CH3)2 D -CH2-S- (CH2) 5-NH-CH2CH2- L CH 3 194 CH3 -CH2-S-(CH2)5-NH-CH2CH2- D CH3 -CH2-S-(CH2)5-NH-C(CH3)3 L -CH2-S-(CH2)5"NH-C(CH3)3 D CH2-0- (CH2) 5-NH-CH3 L CH2-0- (CH2) 5-NH-CH3 D CH2-O- (CH2) 5-NH-CH2CH3 L CH2-0-(CH2)5-NH-CH2CH3 D CH2-0- ( CH2) 5-NH-CH ( CH3) 2 L -155- SUBSTITUTESHEET CH2-0- (CH2) 5-NH-CH (CH3) 2 D CH2-0- (CH2) 5-NH-CH2CH2CH3 L CH2-0- (CH2) 5-NH-CH2CH2CH3 D CH2-0- (CH2) 5-NH-C (CH3) 3 L CH2-0- (CH2) 5-NH-C (CH3) 3 D - (CH2 ) 2-S- (CH2 ) 3-NH-CH3 L - (CH2 ) 2-S- (CH2 ) 3-NH-CH3 D - (CH2 ) 2-S- (CH2 ) 3-NH-CH2CH3 L - (CH2 ) 2-S- (CH2 ) 3-NH-CH2CH3 D - (CH2 ) 2-S- (CH2 ) 3-NH- CH(CH3)2 -(CH2) 2-S- (CH2) 3-NH- D CH(CH3)2 -(CH2) 2-S- (CH2) 3-NH- L CH2CH2-CH3 -(CH2) 2-S- (CH2) 3-NH- D CH2CH2-CH3 215 CH3 - (CH2 ) 2-S" (CH2) 3-NH- C(CH3)3 216 CH3 -(CH2) 2-S- (CH2) 3-NH- D C(CH3)3 -(CH2)2-0-(CH2)3"NH-CH3 L -(CH2)2"0-(CH2)3-NH-CH3 D - (CH2 ) 2-0- (CH2 ) 3-NH-CH2CH3 L -(CH2)2-0-(CH2)3"NH-CH2CH3 D - (CH2) 2-0- (CH2) 3-NH- L CH(CH3)2 222 CH3 -(CH2) 2-0- (CH2) 3-NH- D CH(CH 3 )2 -156- SUBSTΪTUTE SHEET 223 CH3 - (CH2) 2-0- (CH2) 3~NH- CH 2 CH2CH3 224 CH3 -(CH2)2"0-(CH2)3-NH- CH2CH2CH3 225 CH3 -(CH2)2-0-(CH2)3-NH- C(CH 3 )3 226 CH3 - (CH2) 2-0- (CH2) 3-NH- D C(CH 3 )3 227 CH3 -(CH2)2-S-(CH2)2"NH-CH3 L 228 CH3 -(CH2)2-S-(CH2)2"NH-CH3 D 229 CH3 -(CH2)2-S-(CH2)2-NH-CH 2 CH 3 L 230 CH3 -(CH 2 )2-S-(CH 2 )2-NH-CH2CH 3 D 231 CH3 -(CH2)2-S-(CH2)2-NH- L CH(CH3)2 232 CH3 - (CH2) 2-S- (CH2) 2"NH- CH(CH3)2 233 CH3 -(CH 2 )2-S-(CH 2 )2-NH- CH2CH2-CH3 234 CH3 -(CH2)2-S-(CH2)2-NH- CH2CH2-CH3 235 CH3 -(CH2)2-S-(CH2)2-NH- C(CH3)3 236 CH3 - (CH 2 ) 2-S- (CH ) 2-NH- D C(CH 3 )3 237 CH3 - (CH2)2-0- (CH2) 2-NH-CH3 L 238 CH3 - (CH2) 2-0- (CH2) 2-NH-CH3 D 239 CH3 -(CH2)2-0-(CH2)2~NH-CH2CH3 L 240 CH3 -(CH2)2-0-(CH2)2"NH-CH2CH3 D 241 CH3 -(CH 2 )2-0-(CH 2 )2-NH- L CH ( CH 3 )2 -157- SUBSTITUTESHEET 242 CH3 - (CH2) 2-0-(CH2) 2~NH- CH(CH3)2 243 CH3 -(CH2) 2-0-(CH2) 2"NH- CH 2 CH2CH3 244 CH3 - (CH2) 2-0- (CH 2 ) 2"NH- CH 2 CH2CH3 245 CH3 - (CH2) 2-0-(CH2)2"NH- C(CH 3 )3 246 CH3 -(CH2)2-0-(CH2)2~NH- C(CH 3 )3 247 CH3 -(CH2)2-S"(CH2) 4-NH-CH3 L D 248 CH3 -(CH2) 2-S"(CH ) 4-NH-CH3 249 CH3 -(CH2) 2-S- (CH2) 4-NH-CH2CH3 L 250 CH3 - (CH2) 2-S-(CH2) 4-NH-CH2CH3 D 251 CH3 -(CH2)2-S" (CH2) 4-NH- L CH(CH3)2 252 CH3 - (CH2)2-S"(CH2 ) 4-NH- CH(CH3) 2 251 CH3 -(CH2) 2-S"(CH2) 4"NH- CH2CH2-CH3 254 CH3 -(CH2)2-S-(CH2)4-NH- CH2CH2-CH3 255 CH3 -(CH2)2-S-(CH2)4-NH- C(CH 3 )3 256 CH3 -(CH2)2-S-(CH2)4-NH- C(CH3)3 257 CH3 -(CH2)3-NH-CH3 L 258 CH3 - (CH2) 3-NH-CH3 D 259 CH3 -(CH 2 ) 3-NH-CH2CH3 L 260 CH3 -(CH 2 ) 3-NH-CH2CH3 D 261 CH3 -(CH2) 3-NH-CH(CH3) 2 L -158- SUBSTITUTESHEET -159- SUBSTITUTE SHEET -(CH2)6~NH-CH3 D -(CH2)6"NH-CH2CH3 L -(CH2)6-NH-CH2CH3 D -(CH2) 6-NH-CH(CH3)2 L • (CH2)6~NH-CH(CH3)2 D •(CH2) 6-NH-CH 2 CH2CH3 L ■ (CH2) 6-NH-CH 2 CH2CH3 D (CH2)6-NH-C(CH 3 )3 L (CH2)6~NH-C(CH 3 )3 D Example Numbers 301-496 have the same structure as Example Numbers 101-296, respectively, except that J = D-Abu rather than D-Val. Example Numbers 501-696 have the same structure as Example Numbers 101-296, respectively, except that J = D-Phg rather than D-Val. Example Numbers 701-896 have the same structure as Example Numbers 101-296, respectively, except that J = D-Pro rather than D-Val. Example Numbers 901-1096 have the same structure as Example Numbers 101-296, respectively, except that J ~ D-Nle, rather than D-Val. Example Numbers 1101-1296 have the same structure as Example Numbers 101-296, respectively, except that J = D-Norvaline, rather than D-Val.

Claims: CLAIMS WHAT IS CLAIMED IS: 1. A compound of the formula (I) : 0=C NR' (R >2"2 (R 23 )C|n» C(R 21 )R 1 ) n - R 31 (I) or a pharmaceutically acceptable salt or prodrug form thereof wherein: R31 is a C 6 ~Ci 4 saturated, partially saturated, or aromatic carbocyclic ring system substituted with 0-2 R 10 ; or n" and n' are independently 0-3; R! and R 22 are independently selected from the following groups: hydrogen, Cι-C8 alkyl substituted with 0-2 R 11 , C2~C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6-C10 bicycloalkyl substituted with 0-2 R 11 , aryl substituted with 0-2 R^-^, a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 N, S, or 0 heteroatoms, =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 0R 13 , -0C(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 1 Sθ2NR 13 R 14 , -NR 14 S02R 13 , -SO3H, -S02R 13 , -SR 13 , -S(=0)R 13 , -S02NR 13 R 14 , -NR 13 R 14 , -NHC(=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , N0 2 , -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, -OCH2CO2H, 2-(1-morpholino)ethoxy; R and R 21 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R22 and R 23 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 1 and R 2 , where R 21 is H, can alternatively join to form a 5-8 membered carbocyclic ring substituted with 0-2 R 12 ; R 1 is selected from one or more of the following: =0, F, Cl, Br, I, -CF3, -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 0R 13 , -OC(=0)R 13 , -0C(=0)0R 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)0R 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 Sθ2NR 13 R 14 , -NR 1 S02R 13 , -SO3H, -S02R 13 , -SR 13 , -S(=0)R 13 , -S02NR 13 R 14 , -NR 13 R 14 , -NHC(=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , NO2, -C(=0)NH0R 13 , -C (=0)NHNR 13 R 14 , oxime, boronic acid, -OCH2CO2H, 2-(1-morpholino)ethoxy, C1-C5 alkyl, C2-C4 alkenyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C2-C6 alkoxyalkyl, C 3 -C 6 cycloalkoxy, C 1 -C 4 alkyl (substituted with -NR l3 R 14 , -CF 3 , NO2, -S02R 13a , or -S (=0) R 13a ) aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms; R 2 is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, C 3 -C 6 cycloalkoxy, -0C(=0)R 13 , -C(=0)R 13 ,-OC(=0)OR 13 , -OR 13 , -CH2OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 1 C(=0)R 13 , -NR 1 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 1 S02R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2-(1-morpholino)ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF 3 , N0 2 , or -S(=0)R 13a ) ; R 13 is H, C1-C7 alkyl, aryl, -(C1-C6 alkyl)aryl, or C3-C6 alkoxyalkyl; R 13a j_ s C1-C7 alkyl, aryl, -(C1-C6 alkyl)aryl, or C3-C6 alkoxyalkyl; R 14 is OH, H, C1-C4 alkyl, or benzyl; R 21 and R 23 are independently selected from: hydrogen; C 1 -C 4 alkyl, optionally substituted with halogen; C1-C2 alkoxy; benzyl; R 2 is H or Ci-Cβ alkyl; R 1 ^ is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic acid, C 3 -Ce cycloalkox", -OC(=0)R 13 , -C(=0)R 13 ,-OC(=0)OR 13 , -OR 13 , -C__ OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 1 S02NR 13 R 14 , -NR 1 Sθ2R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2-(1-morpholino)ethoxy, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF 3 , NO 2 , or -S(=0)R 13a ); J is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or Ci-Cβ alkyl; R 4 is H or C1-C3 alkyl; R5 hydrogen, C1-C8 alkyl substituted with 0-2 R 11 , C2-C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6-C10 bicycloalkyl substituted with 0-2 R 11 , 5 aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 N, S, or 0 heteroatoms, 10 =0, F, Cl, Br, I, -CF3, -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CH 2 OR 13 , -0C(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -0C(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , 15 -NR 13 C(=0)NR 13 R i4 , -NR 14 Sθ2NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -SR 13 , -S(=0)R 13a , -Sθ2NR 13 R 14 , -NR 13 R 14 , -NHC(=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , NO2, -C(=0)NHOR 13 , -C(=0)NHNR 13 R 14 , oxime, boronic 20 acid, -OCH2CO2H, 2-(1-morpholino)ethoxy, -SC(=NH)NHR 13 , N 3 , -Si(CH 3 ) 3 , (C 1 -C5 alkyl)NHR 16 ; 25 -(Co-Cβ alkyl)X; independently 0,1; -(CH2)mS(CH2)2X, where m = 1,2; and wherein X is defined below; R 3 and R 4 may also be taken together to form (CH 2 ) n X I -CH 2 CHCH 2 f W here R 3 and R^ can also be taken together to form ~(CH2) t - ( = 2-4) or -CH 2 SC (CH 3 ) 2 ~ f or R 4 and R5 can also be taken together to form -(CH2)u~, where u = 2-5; R 16 is selected from: an amine protecting group; 1-2 amino acids; 1-2 amino acids substituted with an amine protecting group; is a D-isomer or L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Cβ alkyl; R 7 is selected from: -(C 1 -C7 alkyl)X; independent ly 0,1; -CH 2 -< )— CH 2 X • _> ■ -(CH2) m O-(Cι-C 4 alkyl) -X, where m = 1,2; -(CH2)m -(Cι-C4 alkyl) -X, where m = 1,2; and X is selected from: _ N(R 13 )R 13, -C(=NH) (NH 2 ), -SC(NH)-NH2; R> and R 7 may also be taken together to form (CH 2 ) π X I ~ CH 2 L is -Y(CH2) V C(=0)-, wherein: Y is NH, N(Cι-C 3 alkyl), 0, or S; and v = 1,2; M is a D-isomer or L-isomer amino acid of structure -NR 17 -CH(R 8 )C(=0)-, wherein: R 17 is H, C1-C3 alkyl; R 8 is -CH2C02R 13 ,-CH2S03R 13a , -CH (CH3) CO2R 13 , -S02NR 13 R 14 , -CH2-boronic acid, -CH2~tetrazole, -NHS0 2 CF3, -CONHNHSO2CF3, -PO(OR 13 ) 2 , -PO(OR 13 )R 13 , -CONHOR 13 , -SO∑NH-heteroaryl, -CH2S02NH-heteroaryl, -SO2NHCOR 13 , -CH2SO2NHCOR 13 , -CONHS02R 13a , -CH 2 CONHSθ2R 13a , -NHS0 2 NHCOR 13a , -NHCONHSO2R 13 , -SO2NHCONR 13 . A compound of Claim 1 of the formula (I) K' / \ M / \ o=c NR' (R 22 (R 23 ) C. C(R 21 )R 1 ) n - _ R» 31 / (I) or a pharmaceutically acceptable salt or prodrug form thereof wherein: R 31 is a C6-C 14 saturated, partially saturated, or aromatic carbocyclic ring system substituted with 0-2 R 10 ; or n" and n* are independently 0-3; R 1 and R 22 are independently selected from the following groups : hydrogen, C1-C8 alkyl substituted with 0-2 R 11 , C2-C8 alkenyl substituted with 0-2 R 11 , C2-C8 alkynyl substituted with 0-2 R 11 , C3-C8 cycloalkyl substituted with 0-2 R 11 , C6-Cχo bicycloalkyl substituted with 0-2 R 11 , aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms, =0, F, Cl, Br, I, -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CHO, -CH 2 OR 13 , -OC(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -S02R 13a , -SR 13 , -S(=0)R 13a , -Sθ2NR 13 R 14 , -CH 2 NR 13 R 14 , -NR 13 R 14 , -NHC(=NH) HR 13 , -C(=NH)NHR 13 , NO 2 ; R 1 and R 21 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 22 and R 23 can alternatively join to form a 5-7 membered carbocyclic ring substituted with 0-2 R 12 ; R 1 and R 2 , where R 21 is H, can alternatively join to form a 5-8 membered carbocyclic ring substituted with 0-2 R 12 ; R 11 is selected from one or more of the following: =0, F, Cl, Br, I, -CF 3 , -CN, -C02R 13 , -C(=0)R 13 , -C(=0)NR 13 R 14 , -CH 2 OR 13 , -OC(=0)R 13 , -OC(=0)OR 13 , -OR 13 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0)NR 13 R 14 , -NR 14 Sθ2NR 13 R 14 , -NR 1 S02R 13a , -SO3H, -S02R 13 , -SR 13 , -S(=0)R 13a , -S02NR 13 R 14 , -CH2NR 13 R 14 , -NR 13 R 14 , -NHC (=NH)NHR 13 , -C(=NH)NHR 13 , =NOR 14 , N0 2 , C1-C5 alkyl, C2-C4 alkenyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C2-C6 alkoxyalkyl, C 1 -C 4 alkyl (substituted with -NR 13 R 14 , -CF3, NO2, -SO2R 13 , or -S(=0)R l3a ) aryl substituted with 0-2 R 12 , a heterocylic ring system substituted with 0-2 R 12 , composed of 5-10 atoms including 1-3 nitrogen, oxygen, or sulfur heteroatoms; R 12 is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , hydroxamic acid, hydrazide, oxime, boronic acid, sulfonamide, formyl, C3-C6 cycloalkoxy, -OC(=0)R 13 , -C (=0)R 13 ,-OC (=0) OR 13 , -OR 13 , -CH2OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 14 C(=0)R 13 , -NR 1 C(=0)OR 13 , -NR 13 C (=0)NR 13 R 14 , -NR 1 S02NR 13 R 14 , -NR 14 S02R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2- (1-morpholino) ethoxy, C1-C4 alkyl (substituted with -NR 13 R 14 , -CF3, N0 2 , or -S(=0)R 13a ); R 13 is H, C1-C7 alkyl, aryl, -(C1-C6 alkyl)aryl, or C3-C6 alkoxyalkyl; &!_. £s OH, H, C1-C4 alkyl, or benzyl; R 21 and R 23 are independently selected from: hydrogen; C -C 4 alkyl, optionally substituted with halogen; C1-C2 alkoxy; benzyl; R 2 is H or Ci-Ca alkyl; R 1 ^ is selected from one or more of the following: phenyl, benzyl, phenethyl, phenoxy, benzyloxy, halogen, hydroxy, nitro, cyano, C1-C5 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C7-C10 arylalkyl, C1-C4 alkoxy, -CO2R 13 , hydroxamic acid, hydrazide, oxime, boronic acid, sulfonamide, formyl, C 3 -Ce cycloalkoxy, -OC(=0)R 13 , -C(=0)R 13 ,-OC(=0)OR 13 , -OR 13 , -CH 2 OR 13 , -NR 13 R 14 , -OC(=0)NR 13 R 14 , -NR 1 C(=0)R 13 , -NR 14 C(=0)OR 13 , -NR 13 C(=0) R 13 R 14 , -NR 14 S02NR 13 R 14 , -NR 1 S02R 13a , -SO3H, -Sθ2R 13a , -S(=0)R 13a , -SR 13 , -S02NR 13 R 14 , C2-C6 alkoxyalkyl, C1-C4 hydroxyalkyl, methylenedioxy, ethylenedioxy, C1-C4 haloalkyl, C1-C4 haloalkoxy, C1-C4 alkoxycarbonyl, C1-C4 alkylcarbonyloxy, C1-C4 alkylcarbonyl, C1-C4 alkylcarbonylamino, -OCH2CO2H, 2- (1-morpholino) ethoxy, C1-C4 alkyl (substituted with -NR 13 R 14 , -CF3, N0 2 , or -S(=0)R 13 ) ; J is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 ) C (R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, C3.-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C1-C6 cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S NH 2 , (CH 2 ) S NHC(=NH) (NH 2 ), (CH 2 ) S NHR 16 , where s - 3-5; R 3 and R5 can be taken together to form -(CH2)t- ( fc = 2-4) or -CH 2 SC(CH 3 ) 2 -; or R 4 and R5 can be taken together to form - (CR2 ) u~r where u = 2-5; R 16 is selected from: an amine protecting group; 1-2 amino acids; 1-2 amino acids subtituted with an amine protecting group; is a D-isomer or L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Cβ alkyl; R 7 is selected from: -(C 1 -C7 alkyl)X; independently 0,1; ~(CH2)mO-(Ci-C4 alkyl)-X, where m = 1,2; ~(CH2)mS-(C 1 -C 4 alkyl)-X, where m = 1,2; and X is selected from: t>13 R^ -N(R 13 )R 13 , -C(=NH) (NH 2 ) -SC(NH)-NH2; R> and R 7 may also be taken together to form (CH 2 ) n X I -CH is -Y(CH2) C(=0)-, wherein: Y is NH, N(Cι-C 3 alkyl), O, or S; and v = 1,2; M is a D-isomer or L-isomer amino acid of structure -NR 17 -CH(R 8 )C(=0)-, wherein: R 17 is H, C 1 -C 3 alkyl; RS is -CH2C02R 13 ,-CH2S03R 13a , -CH(CH3)CO2R 13 , -Sθ2NR 1 R 14 , -CH2~boronic acid, or -CH2~tetrazole. 3. A compound of Claim 1, wherein: R 31 is selected from the group consisting of: (a) a 6 membered saturated, partially saturated or aromatic carbocyclic ring substituted with 0-2 R 10 ; (b) a 8-11 membered saturated, partially saturated, or aromatic fused bicyclic carbocyclic ring substituted with 0-2 R 10 ; or (c) a 14 membered saturated, partially saturated, or aromatic fused tricyclic carbocyclic ring substituted with 0-2 R 10 . 4. A compound of Claim 3, wherein: R 31 is selected from the group consisting of: (a) a 6 membered saturated, partially saturated, or aromatic carbocyclic ring of formula: wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 R 10 ; (b) a 10 membered saturated, partially saturated, or aromatic bicyclic g of formula: wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 R 10 ; (c) a 9 membered saturated, partially saturated, or aromatic bicyclic carbocyclic ring of formula: wherein any of the bonds forming the carbocyclic ring may be a single or double bond, and wherein said carbocyclic ring is substituted independently with 0-2 R 10 . 5. A compound of Claim 4, wherein: R 31 is selected from: wherein the dashed bond may be a single or double bond; wherein R 31 may be substituted independently with 0-2 R 10 ; n" is 0 or 1; n' is 0-3. 6. A compound of Claim 5, or a pharmaceutically acceptable salt or prodrug form thereof, wherein: R 31 is selected from: in wherein R 31 may be substituted independently with 0-2 R 10 ; n" is 0 or 1; n' is 0-2. R 1 and R 22 are independently selected from H, C1-C4 alkyl, phenyl, benzyl, phenyl-(C2-C4)alkyl, C 1 -C 4 alkoxy; R 21 and R 23 are independently H or C 3 .-C 4 alkyl; R 2 is H or Ci-Cs alkyl; R ^ is H, Ci-Cβ alkyl, phenyl, halogen, or C 1 -C 4 alkoxy; J is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, C1-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C1-C6 cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S X where X is -NH or -NHC(=NH) (NH 2 ) and s = 3-5; or R 3 and R5 can be taken together to form -(CH2) t ~ (t = 2-4) or -CH 2 SC(CH 3 ) 2 -;or R 4 and R 5 can be taken together to form -(CH2)u~, where u = 2-5; K is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Cχ-C 8 alkyl; R 7 is -(CH2) P NHC(=NH) (NH2) , where p - 3-5; ere q = 0,1; -(CH2) r X where r = 4-6; (CH2) m S ( CH2)2X, where m = 1,2; (C3-C7 alkyl)-N-(Cι-C 6 alkyl) -(CH2)m-0-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; -(CH2) m -S-(Ci-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2); or (CH 2 ) n X I R 6 and R 7 are taken together to form -CH 2 CHCH 2 - ^ where n = 0,1 and X is -NHC(=NH) (NH2) ; L is -Y(CH2) V C(=0)-, wherein: Y is NH, O, or S; and v = 1,2; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2C02H,-CH2S03H, or -CH(CH3)CO2H; 7. A compound of Claim 6 of the formula (II) wherein: R 1 is H, C1-C4 alkyl, phenyl, benzyl, or phenyl-(C_- C4)alkyl; R 2 is H or methyl; J is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, C1-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C -Cζ cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH.2SCH3, CH2CH2SCH3, (CH 2 ) S X where X is NH 2 or NHC(=NH) (NH 2 ) and s = 3-5; or R 3 and R^ can be taken together to form -CH2CH2CH2-; or R 4 and R^ can be taken together to form -(CH2)u _ , where u = 2-5; is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or Ci-Cβ alkyl; R 7 is -(CH2)pNHC(=NH) (NH2) , where p = 3-5; -(CH2) r X,where r = 4-6; -(CH2) S(CH2)2X, where m = 1,2; -(C3-C7 alkyl) -N-(Cι-C 6 alkyl) - (CH2) m-0- (C 1 -C 4 alkyl) -NH- (Cι-C 6 alkyl) , where m = 1, 2; -(CH2)m-S-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2) , provided that X is not -NH2 when r = 4; or (CH 2 ) n X I R 6 and R7 are taken together to form -CH 2 CHCH 2 - / where n = 0,1 and X is -NHC(=NH) (NH2) ; L is -Y(CH2)vC(=0)-, wherein: Y is NH, 0, or S; and v = 1,2; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2C02H,-CH2S03H, or -CH(CH3)CO2H. 8. A compound of Claim 7 wherein: R 1 is H, C1-C4 alkyl, phenyl, benzyl, or phenyl-(C2-C4)alkyl; R 2 is H or methyl; is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H; R 5 is H, C1-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, C1-C6 cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) S X where X is NH 2 or NHC(=NH) (NH 2 ) and s = 3,4,5; or R 3 and R5 can be taken together to form -CH2CH2CH2-; is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or CH 3 alkyl; R 7 is -(CH2)pNHC(=NH) (NH2) , where p - 3-4; (CH2) r X,where r = 4-6; (CH2)mS(CH2)2X/ where m = 1,2; -(C4-C7 alkyl)-N-(Cι-C6 alkyl) -(CH2)m-0-(Cι-C alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; -(CH2)m-S-(Cι-C 4 alkyl)-NH-(Ci-Cg alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2) , provided that X is not -NH2 when r = 4; or L is -YCH2C(=0)-, wherein: Y is NH or 0; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2CO2H or -CH2SO3H. 9. A compound of Claim 8 wherein: R 1 is H; R 2 is H; J is b-Ala or an L-isomer or D-isomer amino acid of formula -N(R 3 )CH(R 5 )C(=0)-, wherein: R 3 is H and R 5 is H, CH3, CH2CH3, CH(CH3)2, CH(CH 3 )CH 2 CH 3 , CH 2 CH 2 CH 3 , CH 2 CH 2 CH 2 CH 3 , CH CH 2 SCH 3 , CH2CH(CH3) 2 , (CH 2 ) NH 2 ; or R 3 is CH 3 and R 5 is H; or R 3 and R5 can be taken together to form -CH2CH2CH2-. K is an L-isomer amino acid of formula -N(CH 3 )CH(R 7 )C(=0)-, wherein: R 7 is - (CH2 ) 3NHC (=NH) (NH2 ) ; L is -NHCH2C (=0) -; and M is an L-isomer amino acid of formula -NHCH(CH 2 COOH)C(=0)-. 10. A compound of Claim 6 of the formula (III) wherein: R 1 is H, C1-C4 alkyl, phenyl, benzyl, or phenyl-(C1-C )alkyl; R 2 is H or methyl; is b-Ala or an L-isomer or D-isomer amino acid of structure -N(R 3 )C(R 4 ) (R 5 )C(=0)-, wherein: R 3 is H or CH3; R 4 is H or C1-C3 alkyl; R 5 is H, Cχ-C8 alkyl, C3-C6 cycloalkyl, C3-C6 cycloalkylmethyl, Cχ-C cycloalkylethyl, phenyl, phenylmethyl, CH2OH, CH2SH, CH2OCH3, CH2SCH3, CH2CH2SCH3, (CH 2 ) 3 X where X is NH 2 or NHC(=NH) (NH 2 ) and s = 3-5; or R 3 and R 5 can be taken together to form -CH2CH2CH2-; or R 4 and R 5 can be taken together to form -( R2)u~r where u = 2-5; is an L-isomer amino acid of structure -N(R 6 )CH(R 7 )C(=0)-, wherein: R 6 is H or C1-C8 alkyl; R 7 is -(CH2)pNHC(=NH) (NH2) , where p = 3-4; -(CH2) r X, where r = 4-6; ~(CH2)mS(CH2)2X/ where m = 1,2; -(C3-C7 alkyl) -N-(Cι-C 6 alkyl) -(CH2)m-0-(Cι-C 4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; ~(CH2)m-S-(Ci-C4 alkyl)-NH-(Cι-C 6 alkyl), where m = 1,2; and X is -NH2 or -NHC(=NH) (NH2), provided that X is not -NH2 when r = 4; or (CH 2 ) n X I R 6 and R7 are taken together to form -CH 2 CHCH 2 / where n = 0,1 and X is -NHC(=NH) (NH2) ; L is -Y(CH2)vC(=0)-, wherein: Y is NH, 0, or S; and v = 1,2; M is an L-isomer amino acid of structure -NH-CH(R 8 )C(=0)-, wherein: R 8 is -CH2C02H,-CH2S03H, or -CH(CH3)CO2H. 11. A compound of Claim 7 of formula (II) wherein is H; is H; J is b-Ala or an L-isomer or D-isomer amino acid of formula -N(R 3 )CH(R 5 )C(=0) -, wherein: R 3 is H and R 5 is H, CH3, CH2CH3, CH(CH3)2, CH(CH 3 )CH 2 CH 3 , CH CH 2 CH 3 , CH 2 CH CH 2 CH 3 , CH 2 CH 2 SCH 3 , CH2CH(CH3)2, (CH 2 ) 4 NH 2 ; or R 3 is CH 3 and R 5 is H; or R 3 and R^ can be taken together to form -CH2CH2CH2- K is an L-isomer amino acid of formula -N(CH 3 )CH(R 7 )C(=0)-, wherein: R 7 is -(CH2)3NHC(=NH) (NH2) ; L is -NHCH2C(=0)-; and M is an L-isomer amino acid of formula -NHCH(CH 2 COOH)C(=0)-. 12. A compound of Claim 7 which is selected from the group consisting of: the compound of formula (II) : wherein R and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Pro; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ser; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Lys; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is b-Ala; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is b-Ala; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Pro; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Phe; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 is methyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R is methyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R is phenyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 is phenyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is D-NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phg; K is NMeArg; L is Gly; and M is Asp; . the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ile; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Tyr; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Ala; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is Arg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeAmf; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Ala; and M is Asp; the compound of formula (II) wherein R and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is aMeAsp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val;; K is NMeArg; L is Gly; and M is bMeAsp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is NMeAsp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is D-Asp; the compound of formula (II) wherein R 1 is H; R 2 is CH3; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Abu; K is di-NMeOrn; L is Gly; and M is Asp; the compound of formula (III) wherein R and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp. the compound of formula (V) wherein n"=l; R 1 , R 2 , and R 22 are H; J is D-Val; is NMeArg; L is Gly; and M is Asp; the compound of formula (V) wherein n"=0; R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VI) wherein R 2 and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) : wherein R^R 2 , and R 10 are H; R 10a is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ are H; R 10a is I; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ are H; R 10a is I; J is D-Abu; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ are H; R 10 is OMe; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ are H; R 10 is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R ^ 3 - are H; R 10 is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ are H; R 10 is MeO; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ 3 - are H; R 10 is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VIII) : (VIII) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (IX) (IX) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. 13. A compound of Claim 7 which is selected from the group consisting of: the compound of formula (II) : wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is Gly; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Pro; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Lys; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is b-Ala; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is NMeGly; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 is methyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R is methyl (isomer 2) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 is phenyl (isomer 1) ; R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R and R 2 are H; J is D-Val; K is D-NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phg; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ile; K is NMeArg; L is Gly; and M is Asp; the compound of formula (III) : wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (V) : wherein n"=l; R 1 , R 2 , and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (V) wherein n"=0; R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VI) : wherein R 2 and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) : wherein R 1 ,R 2 , and R 10 are H; R 10a is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R , and R 1( ^ are H; R 10a is I; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ are H; R 10a is I; J is D-Abu; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ are H; R 10a is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1 ^ 3 are H; R 10 is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R , and R 1( ^ a are H; R 1 ^ is MeO; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ 3 - are H; R 1 ^ is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Tyr; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeA f; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val;; K is NMeArg; L is Gly; and M is bMeAsp; the compound of formula (II) wherein R 1 is H; R 2 is CH3; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (III) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VIII) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. 14. The compound of Claim 13 selected from the group consisting of: the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-2-aminobutyric acid; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Leu; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ala; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Pro; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Lys; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Nle; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Phe; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Ile; K is NMeArg; L is Gly; and M is Asp; the compound of formula (V) wherein n"=l; R 1 , R 2 , and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VI) : wherein R 2 and R 22 are H; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) : wherein R 1 ,R 2 , and R 10 are H; R 10a is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 10 are H; R 10 is I; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 10 are H; R 10a is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 1 ^ are H; R 10 is Cl; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R 1 ,R 2 , and R 10a are H; R 10 is MeO; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (VII) wherein R^R 2 , and R 1( ^ a are H; R 1 ^ is Me; J is D-Val; K is NMeArg; L is Gly; and M is Asp; the compound of formula (II) wherein R 1 and R 2 are H; J is D-Val;; K is NMeArg; L is Gly; and M is bMeAsp; the compound of formula (VIII) : (VIII) wherein J is D-Val; K is NMeArg; L is Gly; and M is Asp. 15. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 1. 16. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 2. 17. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 3. 18. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 4. 19. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 5. 20. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 6. 21. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 7. 22. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 8. 23. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 9. 24. A method for the treatment of thromboembolic disorders which comprises administering to a host in need of such treatment a therapeutically effective amount of a compound of Claims 10. 25. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 1. 26. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 2. 27. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 3. 28. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 4. 29. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 5. 30. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 6. 31. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 7. 32. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 8. 33. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 9. 34. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of a compound of Claim 10.

Inventors: DEGRADO WILLIAM FRANK, JACKSON SHARON ANNE, MOUSA SHAKER AHMED, PARTHASARATHY ANJU, SWORIN MICHAEL, DEGRADO, WILLIAM, FRANK, JACKSON, SHARON, ANNE, MOUSA, SHAKER, AHMED, PARTHASARATHY, ANJU, SWORIN, MICHAEL
Applicants: DU PONT MERCK PHARMA, THE DU PONT MERCK PHARMACEUTICAL COMPANY
Application year: 1992
Main classification: C07K7
IPC codes: A61K38, A61P7, C07K7, C07K14