Office Action 1: Non-Final Rejection (2022-10-13)
Rejection types: 102 - Lack of Novelty, 101 - Patent-Eligible Subject Matter, 112 - Written Description/Enablement, Double Patenting

CLAIMS:
AMENDMENTS TO THE CLAIMS

Please amend the claims as follows:

1.-15. (Cancelled) 214

16\. (New) 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-Q (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 any five amino acids, and wherein the peptide is 37 or fewer amino acids;
(b) a peptide consisting of the amino acid sequence VKFNKPFVFLMIEQNTK (SEQ ID NO: 1);
(c) a peptide consisting essentially of 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 any five amino acids;
(d) a peptide consisting essentially of the amino acid sequence RFNRPFLR (SEQ ID NO: 4).

(e) a peptide consisting essentially of the amino acid sequence of RRRFNRPFLRRR (SEQ ID NO: 8).

(f) a peptide consisting essentially of the amino acid sequence of VKFNKPFVFLMIEQNTK (SEQ ID NO: 1); and (g) a peptide consisting essentially of the amino acid sequence of FNRPFL (SEQ ID NO: 10).

17\. (New) The composition of claim 1, wherein the peptide further comprises at least one second peptide or protein.

18\. (New) The composition of claim 17, wherein the at least one second protein or peptide is attached to the peptide as a fusion peptide.

19\. (New) The composition of claim 17, wherein the at least one second peptide or protein is an epitope tag or a half-life extender or both.

20\. (New) The composition of claim 1, wherein the peptide comprises one or more D-amino acids.

21\. (New) The composition of claim 1, wherein the peptide consists of 37 amino acid residues or fewer.

22\. (New) The composition of claim 1, wherein the peptide consists of 35 amino acid residues or fewer.

23\. (New) The composition of claim 1, wherein the peptide consists of 22 amino acid residues or fewer.

24\. (New) The composition of claim 1, wherein the peptide consists of 21 amino acid residues or fewer.

25\. (New) The composition of claim 1, further comprising a pharmaceutically acceptable carrier.

26\. (New) The composition of claim 1, wherein the composition is formulated for oral administration.

27\. (New) The composition of claim 1, wherein the composition is formulated for parenteral, intraperitoneal, rectal, cutaneous, nasal, vaginal, inhalant, or ocular administration.

28\. (New) The composition of claim 1, wherein the composition is formulated for intramuscular, intravenous, intraperitoneal, intravesicular, intraarticular, intralesional, or subcutaneous administration.
\-2- -3- -4- 138536-8003.US06/151064246.1 138536-8003.US06/151064246.1

OFFICE ACTION:
DETAILED ACTION
Notice of Pre-AIA  or AIA  Status
The present application is being examined under the pre-AIA  first to invent provisions.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 2/16/21,8/23/21, 12/3/21 were considered by the examiner.
Specification
The disclosure is objected to because of the following informalities: the sequence of SEQ ID NO: 2 in the claims, sequence listing and specification do not match. SEQ ID NO: 2 in the claims has a Q at the end, however SEQ ID NO: 2 in the sequence listing and specification [0080] do not.
Appropriate correction is required.
Drawings
The drawings are objected to because Figs 5-6 and 8-9 are missing labels at the y-axis.  Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 16-17 and 21-28 are rejected under 35 U.S.C. 101 because the claimed invention is not directed to patent eligible subject matter.  Based upon an analysis with respect to the claim as a whole, claims 16-17 and 21-28 do not recite something significantly different than a judicial exception. The rationale for this determination is explained below and is based on the analysis presented in the USPTO’s 2019 Revised Patent subject matter Eligibility Guidance (referred to as 2019 PEG) published January 2019 and the “PEG update” in October 2019.
Claim Interpretation
Claim 16 is drawn to a composition comprising a peptide selected from the group consisting of (a)-(g). Claim 17 claims the composition comprises a second peptide or protein. Claims 21-24 limit the size of the peptide. Claim 25 claims the composition of claim 16 further comprises a pharmaceutically acceptable carrier. Claims 26-28 claim the composition is formulated for oral administration, parenteral….or intramuscular….
Subject Matter Eligibility Test for Products and Processes
Step 1: Is the claim to a process, machine, manufacture, or composition of matter (see, e.g., 79 FR 74621)?
Yes, the instant claims are directed to a statutory patent-eligible subject matter category, namely a composition of matter.
Step 2A  (1): Is the claim directed to a law of nature, a natural phenomenon, or an abstract idea (see, e.g., 79 FR 74621)?
Yes, the claims are directed to a natural phenomenon, the peptides of claim 16 are fragments of naturally occurring proteins.  A BLAST search of the SEQ ID NO: 10 uncovered that SEQ ID NO: 10 is a fragment of a naturally occurring Serpin protein.
PNG
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246
753
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Greyscale
SEQ ID NO: 1 is also a fragment of a naturally occurring protein:
PNG
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219
1138
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Greyscale
Please note that SEQ ID NO: 4 and 8 are also fragments of naturally occurring proteins. Accordingly, the pending claims are directed to a naturally occurring product.
Step 2A (2): Does the Claim recite additional Elements that integrate the judicial Exception into a Practical Application?
No, the claim does not recite additional elements that integrate the judicial exception into a practical application.
Step 2B: Does the claim recite additional elements that amount to significantly more than the judicial exception (see, e.g., 79 FR 74621)?
No, the claims do not recite additional elements that amount to significantly more than the judicial exception. As indicated above, the peptides are fragments that are naturally occurring and the claims do not recite additional elements that amount to significantly more. Although one of ordinary skill in the art would construe the limitation “pharmaceutically acceptable carrier” or “formulated for oral administration” to mean a delivery device suitable for pharmaceutical use and possibly for human administration, this does not render the claim markedly different from what exists in nature. Fragmentation of a protein does not constitute a feature that renders the recited products markedly different from what exists in nature. Even though fragmentation or truncation structurally changes a protein from its natural state, the resultant difference (e.g., “broken” bonds) is not significant enough to render the isolated protein markedly different, because the sequence of the nucleic protein has not been altered.
Factors for determining if the claim directed to a product of nature, as a whole, recites something significantly more than the judicial exception, are provided in the Guidance (74623; see esp. 79 FR 74623 at §I.A.3.b). see also, 79 FR.
In sum, when the relevant considerations are analyzed, they weigh against a significant difference. Accordingly, claims 16-17 and 21-28 do not qualify as eligible subject matter.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b)  CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 16-28 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA  35 U.S.C. 112, the applicant), regards as the invention.
Claims 17 and 20-28 are indefinite because they depend from a cancelled claim (claim 1).
For purposes of examination, claims 17-28 are interpreted to depend from claim 16.
Claim 16 is indefinite because part (a) is internally inconsistent. Part (a) claims the peptide “consisting of the amino acid sequence ..(SEQ ID NO: 1)….wherein the peptide is 37 or fewer amino acids”. The term “consisting of” excludes any element, step of ingredient not specified in the claim (see MPEP 2111.03), however the “wherein the peptide is 37 or fewer amino acids” indicates that SEQ ID NO: 1 can contain addition amino acids in addition to the amino acids of SEQ ID NO: 1 (SEQ ID NO: 1 is 17 amino acids). The claim is internally inconsistent due to the contradictory language used to claim the peptide. The closed language does not allow addition elements to the peptide.
Claim 16 is also indefinite because the sequence of SEQ ID NO:2 in the specification does not match the sequence of SEQ ID NO:2 in the sequence listing filed 12/16/20. SEQ ID NO:2 in the claims has a Q at the end, however the sequence listing does not. It is impossible to determine the metes and bounds of the claims.  For purposes of examination, the SEQ ID NO: 2 is interpreted to have a Q at the end.
Claims 18-24 are also indefinite because:
1) the closed language of Claim 16 (a, b) “consisting of” does not allow addition elements to the peptide. Therefore, the peptide cannot be attached to another peptide, comprise D amino acids or comprise additional amino acids because the closed language of claim 16 does not allow additional elements to the peptide.
2) The claim langue of claims 16 (c-g) “consisting essentially of” language. Applicants define “consisting essentially of” [PGPUB0077]: The phrase “consisting essentially of” is herein meant to define the scope of the peptides to the specified material amino acids, and to only include additional amino acids or changes that do not materially affect the claimed invention's basic and novel characteristics, namely, the anti-inflammatory capacity of the short isolated or synthesized peptides. The definition specifically excludes peptides that have a sequence of a complete Serpin protein, and the definition also specifically excludes peptide sequences that are equal to or longer than 37 amino acids of any naturally occurring Serpin protein.
In the instant case, additional amino acids would necessarily affect the claimed inventions basic characteristics of the peptide. For example adding amino acids to the short peptides of claim will affect the size, MW and charge of the peptide. Adding D-amino acids will affect the structure of the peptide.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of pre-AIA  35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(b) the invention was patented or described in a printed publication in this or a foreign country or in public use or on sale in this country, more than one year prior to the date of application for patent in the United States.
Claims 16-28 are rejected under pre-AIA  35 U.S.C. 102(b) as being anticipated by Gelber et al. (WO2010/081131).
Gelber et al. teach and claim peptide inhibitors containing SEQ ID NO: 6 (FNRPFL). SEQ ID NO: 6 is identical to instantly claimed SEQ ID NO: 10 (claim 1 and p.30, 44).  SEQ ID NO: 6 from Gelber et al. is identical to instant claimed SEQ ID NO: 10 and meets the limitations of Claim 16(g).
With respect to claims 17-19, Gelber claims the peptides are modified peptides, wherein the modified peptides are fusion proteins (claim 4). Gelber et al. teach the peptide inhibitors can be produced as a fusion protein (p. 48). Gelber et al. teach the fusion proteins include the addition of an immunologically active domain, such as an antibody epitope, to facilitate purification of the fusion protein. Other useful fusions include linking of functional domains, such as active sites from enzymes, cellular targeting signals or transmembrane regions (p. 49).
With respect to claim 20, Gelber et al. teach the peptide can be a mimetic of SEQ ID NO: 6 (top of p. 44). Gelber et al. further teach the goal in the design of the mimetic is to reduce the susceptibility of mimetics to cleavage and inactivation of peptidases. Gelber et al. teach the an approach is a variety of modified amino acids, such as D-amino acids (top of p. 45).
With respect to claims 21-24, SEQ ID NO: 6 is 6 amino acid residues in length, meeting the limitation of “35 amino acid residues or fewer”, “22 amino acid residues or fewer” and “21 amino acids or fewer”.
With respect to claim 25, Gelber et al. teach the composition with pharmaceutically acceptable carriers (p. 80, last para.).
With respect to claims 26-28, Gelber et al. teach the composition is formulated for oral and intravenous administration (p. 82). Gelber et al. also teach intranasal administration (p. 83).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA  as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 16-26 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 10,214,562. Although the claims at issue are not identical, they are not patentably distinct from each other. Claims 1,10-12 and 15-16 of the USPN claims peptides for oral administration (SEQ ID NO: 1 and 2) that are identical to instantly claimed SEQ ID NO: 1 and 3, anticipating the limitations of claims 16 and 21-25. Claims 2-5,13 and 17 of USPN claims an oral formulation comprising at least one second peptide or protein, wherein the at least one second protein or peptide is attached to the peptide as a fusion peptide, wherein the second peptide is an epitope tag or half-life extender, wherein the peptide comprises one or more D-amino acids, anticipating the limitations of instant claims 17-20. The USPN claim 9 claims the composition comprises a pharmaceutically acceptable carrier, meeting the limitation of claim 25.
Claims 16-28 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 10,899,797.
Claims 1 and 4-6 of the USPN claims SEQ ID NO: 3 , wherein the peptide is 21 amino acids or few. SEQ ID NO: 3 o the USPN meets the limitations of claims 16 (b-g), 21-24. The USPN also claims the peptide is fused to another peptide or protein, wherein the peptide or protein is an epitope tag, half-life extender or both, wherein the peptide comprises one or more D-amino acids, wherein the composition further comprises a pharmaceutically acceptable carrier (claim 19-12 of USPN), meeting the limitation of instant claims 17-20. The USPN claims composition is administered orally, subcutaneous, intravenous, intramuscular, intraperitoneal, nasally, rectally, intravaginally, parenterally, intracisternally or topically (claims 13-15 of USPN), meeting the limitations of claims 25-28.
Claims 16-28 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-7, 9-10, 13 and 17-1 of copending Application No. 17/215,738.
The copending Application claims SEQ ID NO: 1,4, 8, wherein the peptide has a size of 35 amino acids of less, meeting the limitations of claims 16 and 21-24 (copending Application claims 1-3, 13,21, ). The copending Application claims the oral or subcutaneous administration (copending claims 6, 17), meeting the limitation of claims 26-28. The copending Application claims a second peptide or protein attached to the peptide to form a fusion protein, wherein the second peptide is an epitope tag or half-life extender or both, wherein the peptide comprises one or more D-amino acids (copending claims 7, 9-10, 18-20), meeting the limitations of claims 17-20).
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claims are allowed.


NEXT OFFICE ACTION: DETAILED 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
In the reply filed 1/12/23, Applicants amended claims 16-17 and 20-28.
Claims 16-28 are pending and under consideration.
Examiner’s comment
The Applicants arguments refer to a Declaration filed under 37 CFR 1.132 by Dr. Gelber disclosing the different characteristics of the claimed peptides. However, no such Declaration was submitted. A Declaration filed under 37 CFR 1.132 was submitted disclosing the inventors are the same for the instant application and WO2011/126882 (addressed in detail after the 102 rejection). However, there was no discussion of the properties of the peptides in the Declaration submitted.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 1/12/23 was considered by the examiner.
Specification-Withdrawn
The objection to the specification is withdrawn due to correction of the sequence in the claims.
Drawings
The drawings were received on 1/12/23.  These drawings are acceptable.
Claim Rejections - Withdrawn
The rejection of claims 16-17 and 21-28 under 35 U.S.C. 101 because the claimed invention is not directed to patent eligible subject matter is withdrawn due to Applicants arguments. In particular, Fig. 3 discloses that the claimed sequences are able to reduce TNF-alpha levels compared to the full length protein.
The rejection of claims 17 and 20-28 under 35 U.S.C. 112(b) for being indefinite because they depend from a cancelled claim (claim 1) is withdrawn due to amendment of the claims.
The rejection of claim 16 under 35 U.S.C. 112(b) as indefinite because the sequence of SEQ ID NO:2 in the specification does not match the sequence of SEQ ID NO:2 in the sequence listing filed 12/16/20 is withdrawn due to amendment of claim 16 to the correct sequence.
The rejection of claim 16 under 35 U.S.C. 112(b)  because part (a) is internally inconsistent is withdrawn due to amendment of claim 16 to cancel the limitation “wherein the peptide is 37 or fewer amino acids”.
The rejection of claims 16-24 under 35 U.S.C. 112(b) because the language of Claim 16 (c-g) is unclear is withdrawn due to Applicants arguments.
Claim Objections-NEW
Claim 16 is objected to because of the following informalities: please insert “of” in between “sequence” and “any five amino acids” in part (a) and (c).   Appropriate correction is required.
Claim Rejections - 35 USC § 112-Maintained
The following is a quotation of 35 U.S.C. 112(b):
(b)  CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
The rejection of claims 18-24 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA  35 U.S.C. 112, the applicant), regards as the invention is maintained.
Claims 18-24 are indefinite because: the closed language of Claim 16 (a, b) “consisting of” does not allow additional elements to the peptide. Therefore, the peptide cannot be attached to another peptide, comprise D amino acids or comprise additional amino acids because the closed language of claim 16 does not allow additional elements to the peptide (claims 18-24).
Response to Arguments
Applicant's arguments filed 1/12/23 have been fully considered but they are not persuasive. Applicants argue that the composition is open due to “comprising language”. Applicants argue that the federal circuit has held that closed group designated by the consisting of language is the body of the claim does not limit the open ended comprising language in the claim. Applicants argue that the comprising language of claim 16 allows for additional elements to be attached to the closed list of peptides designated by the “consisting of” language.
This argument is not persuasive. The Examiner agrees that the composition is open. For example, the composition can comprise another peptide as in claim 17. However, the specific peptides of part a) and b) cannot be attached or fused to another peptide because the closed language of the peptide (as in claims 18-24).
Therefore, the rejection is maintained.
Claim Rejections - 35 USC § 102-Maintained
The following is a quotation of the appropriate paragraphs of pre-AIA  35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(b) the invention was patented or described in a printed publication in this or a foreign country or in public use or on sale in this country, more than one year prior to the date of application for patent in the United States.
The rejection of claims 16-28 are rejected under pre-AIA  35 U.S.C. 102(b) as being anticipated by Gelber et al. (WO2010/081131) is maintained.
Gelber et al. teach and claim peptide inhibitors containing SEQ ID NO: 6 (FNRPFL). SEQ ID NO: 6 is identical to instantly claimed SEQ ID NO: 10 (claim 1 and p.30, 44).  SEQ ID NO: 6 from Gelber et al. is identical to instant claimed SEQ ID NO: 10 and meets the limitations of Claim 16(g).
With respect to claims 17-19, Gelber claims the peptides are modified peptides, wherein the modified peptides are fusion proteins (claim 4). Gelber et al. teach the peptide inhibitors can be produced as a fusion protein (p. 48). Gelber et al. teach the fusion proteins include the addition of an immunologically active domain, such as an antibody epitope, to facilitate purification of the fusion protein. Other useful fusions include linking of functional domains, such as active sites from enzymes, cellular targeting signals or transmembrane regions (p. 49).
With respect to claim 20, Gelber et al. teach the peptide can be a mimetic of SEQ ID NO: 6 (top of p. 44). Gelber et al. further teach the goal in the design of the mimetic is to reduce the susceptibility of mimetics to cleavage and inactivation of peptidases. Gelber et al. teach the approach is a variety of modified amino acids, such as D-amino acids (top of p. 45).
With respect to claims 21-24, SEQ ID NO: 6 is 6 amino acid residues in length, meeting the limitation of “35 amino acid residues or fewer”, “22 amino acid residues or fewer” and “21 amino acids or fewer”.
With respect to claim 25, Gelber et al. teach the composition with pharmaceutically acceptable carriers (p. 80, last para.).
With respect to claims 26-28, Gelber et al. teach the composition is formulated for oral and intravenous administration (p. 82). Gelber et al. also teach intranasal administration (p. 83).
Response to Arguments
Applicant's arguments filed 1/12/23 have been fully considered but they are not persuasive. Applicants state that a declaration was submitted to disqualify Gerber et al. as prior art. However, the Declaration is insufficient because the 1) the Declaration references the wrong Gerber et al. reference and 2) the Gerber et al. reference presented above is a 102(b) rejection that was published greater than one year before the effective filing date of the instant invention. Therefore, the rejection is maintained.
Response to Amendment
The Declaration under 37 CFR 1.132 filed 1/12/23 is insufficient to overcome the rejection of claims 16-287 based upon Gerber et al. (WO2010/081131) as set forth in the last Office action because the Declaration is not addressing the correct reference. The Declaration states that the inventors are the same for the instant application and WO2011/126882. However, the reference used in the 102(b) rejection above is WO2010/081131 and was published over one year before the effective filing date of the instant application.
Double Patenting-Maintained
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA  as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
The rejection of claims 16-26 on the grounds of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 10,214,562 is maintained. Although the claims at issue are not identical, they are not patentably distinct from each other. Claims 1,10-12 and 15-16 of the USPN claims peptides for oral administration (SEQ ID NO: 1 and 2) that are identical to instantly claimed SEQ ID NO: 1 and 3, anticipating the limitations of claims 16 and 21-25. Claims 2-5,13 and 17 of USPN claims an oral formulation comprising at least one second peptide or protein, wherein the at least one second protein or peptide is attached to the peptide as a fusion peptide, wherein the second peptide is an epitope tag or half-life extender, wherein the peptide comprises one or more D-amino acids, anticipating the limitations of instant claims 17-20. The USPN claim 9 claims the composition comprises a pharmaceutically acceptable carrier, meeting the limitation of claim 25.
The rejection of claims 16-28 on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 10,899,797 is maintained.
Claims 1 and 4-6 of the USPN claims SEQ ID NO: 3 , wherein the peptide is 21 amino acids or few. SEQ ID NO: 3 o the USPN meets the limitations of claims 16 (b-g), 21-24. The USPN also claims the peptide is fused to another peptide or protein, wherein the peptide or protein is an epitope tag, half-life extender or both, wherein the peptide comprises one or more D-amino acids, wherein the composition further comprises a pharmaceutically acceptable carrier (claim 19-12 of USPN), meeting the limitation of instant claims 17-20. The USPN claims composition is administered orally, subcutaneous, intravenous, intramuscular, intraperitoneal, nasally, rectally, intravaginally, parenterally, intracisternally or topically (claims 13-15 of USPN), meeting the limitations of claims 25-28.
The rejection of claims 16-28 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-7, 9-10, 13 and 17-1 of copending Application No. 17/215,738 is maintained.
The copending Application claims SEQ ID NO: 1,4, 8, wherein the peptide has a size of 35 amino acids of less, meeting the limitations of claims 16 and 21-24 (copending Application claims 1-3, 13,21, ). The copending Application claims the oral or subcutaneous administration (copending claims 6, 17), meeting the limitation of claims 26-28. The copending Application claims a second peptide or protein attached to the peptide to form a fusion protein, wherein the second peptide is an epitope tag or half-life extender or both, wherein the peptide comprises one or more D-amino acids (copending claims 7, 9-10, 18-20), meeting the limitations of claims 17-20).
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 1/12/23 have been fully considered but they are not persuasive. Applicants request the rejections be held in abeyance until one or more claims are found allowable.
The rejections are maintained because there is no indication of allowable subject matter.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL.  Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action.  In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action.  In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.

CITED REFERENCE SUMMARIES: Ref WO2010081131: Claims:
An isolated and modified peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 6, SEQ ID NO:7, R[S/K]XXPP and SXXPP, wherein F= phenylalanine, N= asparagine, R= arginine, P= proline, L= leucine, M= methionine, S= serine, G= glycine, K= lysine, V= valine, and X= any amino acid.
The isolated and modified peptide of claim 1, wherein the modified peptide comprises a chemical modification.
The isolated and modified peptide of claim 2, wherein the chemical modification is selected from the group consisting of addition of a chemical functional group, glycosylation, phosphorylation, or peptide cyclization.
The isolated and modified peptide of any of the preceding claims, wherein the modified peptide comprises a fusion protein.
A derivative or analog of SEQ ID NO: 1.
A pharmaceutical composition comprising a modified peptide or a peptide fragment of any of the preceding claims and a pharmaceutically acceptable carrier.
A use of a pharmaceutical composition of claim 6 for inhibiting one or more kinases in a subject.
The use according to claim 7, wherein the one or more kinases is selected from the group consisting of kinases listed in TablelÎ´ or Table 20.
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.
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 APP-17_215738: Claims:
A method of treating a disease associated with a cytokine storm, comprising administering to a human subject affected with the disease a pharmaceutical composition comprising a peptide selected from the group consisting of: (a) a peptide comprising the amino acid sequence (SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (b) a peptide consisting essentially of the amino acid sequence (SEQ ID NO: 4) RFNRPFLR. (c) a peptide consisting essentially of the amino acid sequence of (SEQ ID NO: 8) RRRFNRPFLRRR. (d) a peptide consisting essentially of the amino acid sequence of (SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (e) a peptide consisting essentially of the amino acid sequence of (SEQ ID NO: 10) FNRPFL; (f) a peptide comprising (SEQ ID NO: 57) VKFNKPFVFL[Nle]IEQNTK. wherein the peptide has a size of 35 amino acids or less.
A method of treating a disease associated with a cytokine storm, comprising administering to a human subject affected with the disease a pharmaceutical composition comprising a peptide selected from the group consisting of: (a) a peptide comprising the amino acid sequence
(a) a peptide comprising the amino acid sequence
(SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (b) a peptide consisting essentially of the amino acid sequence
(b) a peptide consisting essentially of the amino acid sequence
(SEQ ID NO: 4) RFNRPFLR. (c) a peptide consisting essentially of the amino acid sequence of
(c) a peptide consisting essentially of the amino acid sequence of
(SEQ ID NO: 8) RRRFNRPFLRRR. (d) a peptide consisting essentially of the amino acid sequence of
(d) a peptide consisting essentially of the amino acid sequence of
(SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (e) a peptide consisting essentially of the amino acid sequence of
(e) a peptide consisting essentially of the amino acid sequence of
(SEQ ID NO: 10) FNRPFL; (f) a peptide comprising
(f) a peptide comprising
(SEQ ID NO: 57) VKFNKPFVFL[Nle]IEQNTK. wherein the peptide has a size of 35 amino acids or less.
wherein the peptide has a size of 35 amino acids or less.
The method of claim 1, wherein the disease associated with a cytokine storm is selected from the group consisting of: acute myocardial infarction (AMI); gout; stroke; heart surgery complications; and traumatic brain injury.
acute myocardial infarction (AMI); gout; stroke; heart surgery complications; and traumatic brain injury.
A method of reducing infarct size in a human subject in need of treatment therefor, comprising administering to the human subject a pharmaceutical composition comprising a peptide selected from the group consisting of: (a) a peptide comprising the amino acid sequence (SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (b) a peptide consisting essentially of the amino acid sequence (SEQ ID NO: 4) RFNRPFLR. (c) a peptide consisting essentially of the amino acid sequence of (SEQ ID NO: 8) RRRFNRPFLRRR. (d) a peptide consisting essentially of the amino acid sequence of (SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (e) a peptide consisting essentially of the amino acid sequence of FNRPFL (SEQ ID NO: 10); and (f) a peptide comprising (SEQ ID NO: 57) VKFNKPFVFL[Nle]IEQNTK. wherein the peptide has a size of 35 amino acids or less.
A method of reducing infarct size in a human subject in need of treatment therefor, comprising administering to the human subject a pharmaceutical composition comprising a peptide selected from the group consisting of: (a) a peptide comprising the amino acid sequence
(SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (b) a peptide consisting essentially of the amino acid
(b) a peptide consisting essentially of the amino acid
sequence (SEQ ID NO: 4) RFNRPFLR. (c) a peptide consisting essentially of the amino acid sequence of
(SEQ ID NO: 1) VKFNKPFVFLMIEQNTK; (e) a peptide consisting essentially of the amino acid sequence of FNRPFL (SEQ ID NO: 10); and (f) a peptide comprising
(e) a peptide consisting essentially of the amino acid sequence of FNRPFL (SEQ ID NO: 10); and
(SEQ ID NO: 57) VKFNKPFVFL[Nle]IEQNTK.
The method of claim 3, wherein the human subject in need of a reduction in infarct size is a subject in need of treatment for a disease selected from the group consisting of: acute myocardial infarction (AMI); ischemia; stroke; traumatic brain injury; and toxic shock.
acute myocardial infarction (AMI); ischemia; stroke; traumatic brain injury; and toxic shock.
The method of claim 1, wherein the pharmaceutical composition is administered orally or subcutaneously to the human subject.
The method of claim 1, wherein the pharmaceutical composition further comprises at least one second peptide or protein attached to the peptide to form a fusion protein.
The method of claim 7, wherein the at least one second peptide or protein is an epitope tag or a half-life extender or both.
The method of claim 1, wherein the peptide comprises one or more D-amino acids.
The method of claim 1, wherein the peptide consists of 22 amino acid residues, 21 amino acid residues, or fewer.
The method of claim 3, wherein the pharmaceutical composition is administered orally or subcutaneously to the human subject.
The method of claim 3, wherein the pharmaceutical composition further comprises at least one second peptide or protein attached to the peptide to form a fusion protein.
The method of claim 18, wherein the at least one second peptide or protein is an epitope tag or a half-life extender or both.
The method of claim 3, wherein the peptide comprises one or more D-amino acids.
The method of claim 3, wherein the peptide consists of 22 amino acid residues, 21 amino acid residues, or fewer.
A pharmaceutical composition comprising a peptide comprising the amino acid sequence of VKFNKPFVFL[Nle]IEQNTK (SEQ ID NO: 57), and a pharmaceutically acceptable carrier, wherein the peptide has a size of 35 amino acids or less.
The pharmaceutical composition of claim 22, wherein the peptide consists of 22 amino acid residues, 21 amino acid residues, or fewer.
The pharmaceutical composition of claim 22, wherein the composition is formulated into a dosage form suitable for oral, parenteral, intraperitoneal, rectal, subcutaneous, nasal, vaginal, inhalant, dermal, or ocular administration.
The pharmaceutical composition of claim 22, wherein the peptide is fused to an epitope tag, or a half-life extender.
The pharmaceutical composition of claim 22, wherein the peptide is modified by PEGylation.
The pharmaceutical composition of claim 22, wherein the N-terminus of the peptide is acetylated, the C-terminus of the peptide is amidated, or both.