Office Action 5: Notice of Allowance (2024-12-26)

CLAIMS:
AMENDMENTS TO THE CLAIMS

Please amend claims 16, 18, and 20-24. Following is a complete listing of the

claims pending in the application, as amended. This listing of claims will replace, without

prejudice, all prior versions and listings of the claims in the application.

1.-15. (Cancelled)214

16\. (Currently Amended) A composition comprising a peptide selected from the group consisting of:
(a) a peptide consisting of the amino acid sequence X1-Z1-F-N-K-P-F-X2-Z2- X3-Z3 (SEQ ID NO: 2), wherein X1 is VorL;X2 is V, L or M;
X3 is M, I or V;
Z1 is any amino acid;
Z2 is a sequence of any two amino acids; and
Z3 is a sequence of any five amino acids;
(bs) a peptide consisting essentially of the amino acid sequence RFNRPFLR (SEQ ID NO: 4);and
(cd) a peptide consisting essentially of the amino acid sequence of RRRFNRPFLRRR (SEQ ID NO: 8)
 .

17\. (Previously Presented) The composition of claim 16, further comprising at least one second peptide or protein.

18\. (Currently Amended) The composition of claim 17, wherein the at least one second protein or peptide is attached to the peptide of (bs)\_or-(ce) as a fusion peptide.

19\. (Previously Presented) The composition of claim 18, wherein the at least one second peptide or protein is an epitope tag or a half-life extender or both.

20\. (Currently Amended) The composition of claim 16, wherein the peptide of (be)-(ce) further comprises one or more D-amino acids.

21\. (Currently Amended) The composition of claim 16, wherein the peptide of (be)-(ce) consists of 37 amino acid residues or fewer.

22\. (Currently Amended) The composition of claim 16, wherein the peptide of (bs)-(ce) consists of 35 amino acid residues or fewer.

23\. (Currently Amended) The composition of claim 16, wherein the peptide of (bs)-(ce) consists of 22 amino acid residues or fewer.

24\. (Currently Amended) The composition of claim 16, wherein the peptide of (bs)-(ce) consists of 21 amino acid residues or fewer.

25\. (Previously Presented) The composition of claim 16, further comprising a pharmaceutically acceptable carrier.

26\. (Previously Presented) The composition of claim 16, wherein the composition is formulated for oral administration.

27\. (Previously Presented) The composition of claim 16, wherein the composition is formulated for parenteral, intraperitoneal, rectal, cutaneous, nasal, vaginal, inhalant, or ocular administration.

28\. (Previously Presented) The composition of claim 16, wherein the composition is formulated for intramuscular, intravenous, intraperitoneal, intravesicular, intraarticular, intralesional, or subcutaneous administration.

OFFICE ACTION:
Notice of Pre-AIA  or AIA  Status
The present application is being examined under the pre-AIA  first to invent provisions.
Status of the Claims
Claims 16-28 are pending.
In the reply filed 9/10/24, Applicants amended claims 16, 18 and 20-24.
The 102(b) and 103 rejection of claims 16-19, 21-23 and 25 over Cercek et al. is withdrawn due to amendment of claim to cancel SEQ ID NO: 1.
The rejection of claims 16-28 on the grounds of nonstatutory double patenting over USPN 10,899,797; 9,951,104; 8,975,224 and Applications 17/215,738 and 18/148,942 is withdrawn due to amendment of claim 16 to cancel SEQ ID NO: 1.
The rejection of claims 16-28 on the grounds of nonstatutory double patenting over USPN 10,214,562 is withdrawn due to filing of a TD.
Claims 16-28 are allowed in the Notice of Allowance herewithin.
Terminal Disclaimer
The terminal disclaimer filed on 12/5/24 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of USPN 10,214,562 has been reviewed and is accepted.  The terminal disclaimer has been recorded.
Reasons for Allowance
The following is an examiner’s statement of reasons for allowance: Claims 16-28 are allowed. The closest prior art of Cercek et al. (previously presented). However, Cercek et al. does not teach or suggest the peptides of amended claim 16. Cercek et al. does not teach or suggest SEQ ID NO: 2, 4 or 8. A search of the prior art did not uncover any reference that taught SEQ ID NO: 2, 4 and 8.  Therefore, claims 16-28 are free of the art and are novel.
Any comments considered necessary by applicant must be submitted no later than the payment of the issue fee and, to avoid processing delays, should preferably accompany the issue fee.  Such submissions should be clearly labeled “Comments on Statement of Reasons for Allowance.”
Conclusion
Claims 18-28 are allowed.

APPLICANT REBUTTAL: REMARKS/ARGUMENTS
Claims 16-28 were pending when the present Office Action was mailed on June 11, 2024 (hereinafter "Office Action" or "OA").
In this response, claims 16, 18, and 20-24 have been amended to address informalities and to further clarify certain features of these claims. Support for these amendments can be found in the application as originally filed, and in the original listing of the claims. No claims have been added or canceled. The foregoing amendments are made solely to expedite prosecution of this application and without prejudice to pursuing these claims in unamended or other forms in a continuation or other application. Applicant respectfully requests entry of this amendment and upon entry, claims 16-28 will remain pending.
l.    Response to the Section 102 Rejections
The Office Action rejected claims 16-28 under 35 U.S.C. § 102(b) as allegedly being anticipated by U.S. Patent No. 5,270,171 ("Cercek"). OA at 4. The Office Action stated that
Cercek et al. teach the SCM peptide of X1-I-P-P-E-V-K-F-N- K-P-F-V-F-L-M-I-E-Q N-T-K-S-P-L-F-M-G-K (claim 27). The
peptide of Cercek et al. comprises instantly claimed SEQ ID
NO: 1 (claim 16 (e)) (please see bolded amino acids). Id.
Without conceding to the rejection, and solely to advance prosecution, Applicant has amended claim 1 to recite "A composition comprising a peptide selected from the group consisting of: (a) a peptide consisting of the amino acid sequence X1-Z1-F-N-K- P-F-X2-Z2-X3-Z3 (SEQ ID NO: 2), ...; (b) a peptide consisting essentially of the amino acid sequence RFNRPFLR (SEQ ID NO: 4); and (c) a peptide consisting essentially of the amino acid sequence of RRRFNRPFLRRR (SEQ ID NO: 8)." The SCM peptide from Cercek is not encompassed by amended claim 16. As such, the novelty rejection over
claim 16 is moot. Claims 17-28 depend from and incorporate the features of claim 16. Therefore, Applicant requests withdrawal of the §102 rejections over claims 16-28. II.    Response to the Section 103 Rejections
A.   Cercek
The Office Action rejected claims 16-19 and 21-28 under 35 U.S.C. § 103(a) as allegedly being unpatentable over Cercek. OA at 6. The Office Action stated Cercek et al. does not teach the specific peptides consist of 21 or fewer amino acids or formulated for oral, parenteral, intramuscular...or  subcutaneous  administration  (the limitations of claims 24-28). However, the teachings of Cercek
et al. are suggestive of the limitations. OA at 6.
The Office Action also stated that
With respect to claims 26-28, Cercek et al. teach the SCM peptides in water (Example 3, col. 42; Example 5, col. 44).
Please note that the limitation "formulated for..." is regarded that "intended use" of a composition or product will not further
limit claims drawn to a composition or product. OA at 7.
Even if the Office Action's characterization of Cercek is correct, which Applicant does not concede, Cercek still does not teach or suggest "[a] composition comprising a peptide selected from the group consisting of: (a) a peptide consisting of the amino acid sequence X1-Z1-F-N-K-P-F-X2-Z2-X3-Z3 (SEQ ID NO: 2), ...; (b) a peptide consisting
essentially of the amino acid sequence RFNRPFLR (SEQ ID NO: 4); and (c) a peptide consisting essentially of the amino acid sequence of RRRFNRPFLRRR (SEQ ID NO: 8)," as recited in claim 16. Therefore, claim 16 is not obvious over Cercek. Claims 17-19 and 21-28 depend from and incorporate each and every feature of independent claim 16. Applicant requests withdrawal of the §103 rejection of claims 16-19 and 21-28 over Cercek.
B.   Cercek and Lifetein
The Office Action also rejected claims 16-28 under 35 U.S.C. § 103(a) as allegedly
being unpatentable over Cercek and Lifetein.com (www.lifetein.com/blog/d-amino-acid- peptides-to-resist-common-proteases/) ("Lifetein"). OA at 7.
As noted above, claim 16 is not obvious in view of Cercek at least because Cercek
does not teach or suggest the features of claim 16. The Office Action relies on Lifetein for allegedly "teach[ing] that design of D-peptides have been applied to increase bioactive peptides resistance to endogenous enzymes, as well as their bioavailability." Id.
However, Lifetein fails to cure at least the above noted deficiencies of Cercek to support a prima facie § 103 rejection of independent claim 16. Claims 17-28 ultimately depend from and incorporate each and every feature of claim 16. Accordingly, dependent claims 16-28 are allowable over the combination of Cercek and Lifetein and the §103 rejections
over claims 16-28 should be withdrawn.
III.  Response to the Double-Patenting Rejection
Claims 16-26 were rejected on the ground of nonstatutory obviousness-type
double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 10,214,562;
claims 1-15 of U.S. Patent No. 10,899,797; claims 1-9 of U.S. Patent No. 9,951,104; and
claims 1-8 of U.S. Patent No. 8,975,224.
Claims 16-28 were provisionally rejected on the ground of nonstatutory
obviousness-type double patenting as being unpatentable over 1,3-4, 6-7, 9-10, 13, and 17-27 of copending Application No. 17/215,738 (U.S. Application Publication No.
2021/0369822); claims 1,8, 10-13, 22-23 and 26-27 of copending Application No.
18/148,942 (U.S. Application Publication No. 2023/04006906); and claims 1-16 of
copending Application No. 18/582,061.
As discussed above, independent claim 16 has been amended. The rejections on
the grounds of nonstatutory double patenting are obviated and therefore traversed. MPEP
§ 804(I)(B)(1).
CONCLUSION


CITED REFERENCE SUMMARIES: Ref US10899797: Claims:
1. A method of decreasing serum TNF-α levels in a human subject comprising administering to the subject a composition comprising a peptide wherein the peptide comprises the amino acid sequence
X1-Z1-F-N-X2-P-F-X3-Z2-X4-Z3-X5 (SEQ ID NO: 3), wherein
X1 is V or L;
X2 is K or R;
X3 is V, L or M;
X4 is M, I or V;
X5 is K or Q;
Z1 is any amino acid;
Z2 is a sequence of any two amino acids; and
Z3 is a sequence of any five amino acids; and wherein the peptide is 21 or fewer amino acids in length.
2. The method of claim 1, wherein the subject is administered the composition in an amount that results in at least 50% reduction of the TNF-α levels compared to the TNF-α levels in the subject prior to administering the peptide.
3. The method of claim 2, wherein reduction of the TNF-α levels is at least 75%.
4. The method of claim 1, wherein the peptide comprises the amino acid sequence of any one of:
(SEQ ID NO: 1)
                 
                   
                  VKFNKPFVFLMIEQNTK;
                 
                   
                   
                 
                   
                  (SEQ ID NO: 16)
                 
                   
                  VKFNKPFVFLMIAAATK;
                 
                   
                   
                 
                   
                  (SEQ ID NO: 29)
                 
                   
                  IPPEVKFNKPFVFLMIEQNTK;
                 
                   
                   
                 
                   
                  (SEQ ID NO:44)
                 
                   
                  VRFNRPFLMIIVPTDTQ; or
                 
                   
                   
                 
                   
                  (SEQ ID NO:31)
                 
                   
                  TRTIVRFNRPFLMIIVPTDTQ;
                 
            
                
                
                
                
                
                
                
                
                
                
                
                
                
                
              
            
          
        
        and is 21 or fewer amino acids in length.
5. The method of claim 4, wherein the peptide consists of the amino acid sequence of any one of:
(SEQ ID NO: 1)
                 
                   
                  VKFNKPFVFLMIEQNTK;
                 
                   
                   
                 
                   
                  (SEQ ID NO: 16)
                 
                   
                  VKFNKPFVFLMIAAATK; or
                 
                   
                   
                 
                   
                  (SEQ ID NO:44)
                 
                   
                  VRFNRPFLMIIVPTDTQ.
6. The method of claim 5, wherein the peptide consists of the amino acid sequence of VKFNKPFVFLMIEQNTK (SEQ ID NO: 1).
7. The method of claim 1, wherein the decreasing serum TNF-α levels in the human subject treats sepsis.
8. The method of claim 7, wherein the sepsis is associated with a burn or acute radiation.
9. The method of claim 1, wherein the peptide is fused to at least one second peptide or protein.
10. The method of claim 9, wherein the at least one second peptide or protein is an epitope tag, a half-life extender, or both.
11. The method of claim 1, wherein the peptide comprises one or more D-amino acids.
12. The method of claim 1, wherein the composition further comprises one or more pharmaceutically acceptable carriers.
13. The method of claim 1, wherein the composition is administered orally.
14. The method of claim 1, wherein the composition is administered by subcutaneous, intravenous, intramuscular, or intraperitoneal injection.
15. The method of claim 1, wherein the composition is administered nasally, rectally, intravaginally, parenterally, intracisternally or topically.
Ref US10214562: Claims:
1. A method of improving glycemic control in a subject having hyperglycemia comprising:
administering to the subject having hyperglycemia an oral formulation comprising a peptide selected from the group consisting of:
(a) a peptide comprising the amino acid sequence X1-Z1-F-N-K-P-F-X2-Z2-X3-Z3 (SEQ ID NO: 2), wherein
X1 is V or L;
X2 is V, L or M;
X3 is M, I or V;
Z1 is any amino acid;
Z2 is a sequence of any two amino acids; and
Z3 is a sequence of any five amino acids, and wherein the peptide is 21 or fewer amino acids long; and

(b) a peptide comprising the amino acid sequence VKFNKPFVFLMIEQNTK (SEQ ID NO: 1) and wherein the peptide is 21 or fewer amino acids long.
2. The method of claim 1, wherein the oral formulation further comprises at least one second peptide or protein.
3. The method of claim 2, wherein the at least one second protein or peptide is attached to the peptide as a fusion peptide.
4. The method of claim 2, wherein the at least one second peptide or protein is an epitope tag or a half-life extender or both.
5. The method of claim 1, wherein the peptide comprises one or more D-amino acids.
6. The method of claim 1, wherein the subject having hyperglycemia is affected with type II diabetes or type I diabetes.
7. The method of claim 6, wherein the subject having hyperglycemia is affected with type I diabetes.
8. The method of claim 1, wherein the peptide causes a 75% decrease in serum TNF-α levels when administered in an effective amount to a human subject.
9. The method of claim 1, wherein the oral composition further comprises a pharmaceutically acceptable carrier.
10. A method of improving glycemic control in a subject having hyperglycemia comprising:
administering to the subject having hyperglycemia an oral formulation comprising:
(a) a peptide consisting of the amino acid sequence of VKFNKPFVFLMIEQNTK (SEQ ID NO: 1); or
(b) a peptide consisting of the amino acid sequence of VKFNKPFVFLMIEQNTK (SEQ ID NO: 1) combined with the amino acid sequence of at least one second peptide or protein, wherein the second peptide or protein is an epitope tag or a half-life extender or both.
11. The method of claim 1, wherein the peptide comprises the amino acid sequence VKFNKPFVFLMIEQNTK (SEQ ID NO: 1) and is 21 or fewer amino acids long.
12. The method of claim 11, wherein the peptide consists of the amino acid sequence of IPPEVKFNKPFVFLMIEQNTK (SEQ ID NO: 29).
13. The method of claim 11, wherein the oral formulation further comprises at least one second peptide or protein.
14. The method of claim 13, wherein the subject having hyperglycemia is affected with type II diabetes or type I diabetes.
15. The method of claim 1 wherein the peptide comprises the amino acid sequence X1 -Z1-F-N-K-P-F-X2-Z2-X3-Z3 (SEQ ID NO: 2), wherein:
X1 is V or L;
X2 is V, L or M;
X3 is M, I or V;
Z1 is any amino acid;
Z2 is a sequence of any two amino acids; and
Z3 is a sequence of any five amino acids, and wherein the peptide is 21 or fewer amino acids long.
16. The method of claim 15 wherein the peptide comprises the amino acid sequence of:
(a) VKFNKPFVFLMIAAATK (SEQ ID NO: 16);
(b) VKFNKPFVFLMIEQAAA (SEQ ID NO:17);
(c) VAFNKPFVFLMIEQNTK (SEQ ID NO:53);
(d) VKFNKPFVFLMIEQNAK (SEQ ID NO:55); or
(e) VKFNKPFVFLMIEQNTA (SEQ ID NO:56), and is 21 or fewer amino acids long.
17. The method of claim 15, wherein the oral formulation further comprises at least one second peptide or protein.
18. The method of claim 15, wherein the subject having hyperglycemia is affected with type II diabetes or type I diabetes.