DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
Response to Arguments
Applicant's arguments filed 4/15/2026 regarding the claim rejections under 35 U.S.C. 112(b) have been fully considered and are persuasive. The rejections have been withdrawn in light of the arguments in the Remarks, Pg 16, last paragraph.
Applicant’s arguments filed 4/15/2026 regarding the claim rejections under 35 U.S.C. 102(a)(2) have been fully considered and are persuasive. The rejections have been withdrawn in light of the statement in the Remarks, Pg 14, disqualifying US 2022/0298218 A1 as prior art under 120(b)(2)(C).
Applicant's arguments filed 4/15/2026 regarding the claim rejections under 35 U.S.C. 103 have been fully considered but they are not persuasive.
The Applicant’s position is that the 35 U.S.C. 103 rationale 1) relies on impermissible hindsight, 2) ignores the breadth and different purpose of Just, and 3) fails to articulate any teaching or motivation that would have led one skilled in the art to arrive at the instant Formula A, which is a GIPR antagonist rather than an agonist.
Regarding 1), in response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
In the instant case, Applicants have not pointed to any facet of the rejection that is not in the cited references. Claim 86 is drawn to a GIP peptide analogue with GIPR antagonistic activity. One skilled in the art would recognize that a peptide antagonist would need to engage or directly bind to GIPR. Thus, peptides that can interact with GIPR, including GIP, would be a useful starting point glean such structural information, which is taught in the prior art by Just. Further, Rosenkilde teaches GIP analogue antagonists wherein removal of the first 3 amino acids of GIP(1-30) confers the analogue with antagonistic properties; Rosenkilde also teaches the attachment of fatty acid molecule to increase the analogue’s half-life while maintaining its antagonistic properties. As these teachings qualify as prior art, the rationale for the rejection under 35 U.S.C. 103 does not rely on impermissible hindsight.
Regarding 2), as stated in the prior Office Action and reiterated herein, Just teaches GIP analogues wherein certain positions are variable and can be occupied by a few different amino acids. However, each position is well-defined, and none of the variable positions recite endlessly long lists of possibilities. Thus, it would be obvious to try each and every combination of amino acids, ultimately yielding the instant Formula A of claim 86. See MPEP 2143(E).
Moreover, regarding the different purpose of Just, as explained above, one skilled in the art would recognize that a peptide antagonist would need to engage or directly bind to GIPR. Thus, examining peptides that can interact with GIPR, including GIP, would be a useful starting point to glean such structural information, which is taught in the prior art by Just. One skilled in the art interested in making a peptide analogue with antagonistic activity towards GIPR would then consider teachings in the art that would confer antagonistic activity, which is taught by Rosenkilde.
Regarding 3), in response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007).
In this case, as stated above, one skilled in the art would recognize that a peptide antagonist would need to engage or directly bind to GIPR. Thus, peptides that can interact with GIPR, including GIP, would be a useful starting point glean such structural information, which is taught by Just. Further, Rosenkilde teaches GIP analogue antagonists wherein removal of the first 3 amino acids of GIP(1-30) confers the analogue with antagonistic properties; Rosenkilde also teaches the attachment of fatty acid molecule to increase the analogue’s half-life while maintaining its antagonistic properties. These teachings have been articulated in the prior Office Action and are reiterated herein below.
Applicant’s request that the double patenting rejections be held in abeyance is noted but they have been maintained/modified herein.
Election/Restrictions
Applicant’s election without traverse of Group I, claims 86-105, drawn to a glucose-dependent insulinotropic peptide (GIP) analogue consisting of amino acid SEQ ID NO: 4; and the species SEQ ID NO: 18 C16-diacid/16K in the reply filed on 6/20/2025 is acknowledged.
Claim Status
Claims 86-114 are pending under examination on the merits. Claims 86, 88-89, 91, 95, are currently amended. Claims 87, 90, 94, 97-99, 101-102 107, and 109-114 were previously presented. Claims 1-85, 92, 93, and 96 are cancelled. Claims 100, 104-106, and 108 are withdrawn as non-elected species (claims 100, 104, 105, and 108) and inventions (claim 106).
Priority
The instant application is the 371 national stage entry of PCT/EP2020/084487, filed 12/3/2020, which claims priority to EP20179259.5, filed 6/10/2020, and PCT/EP2019/083506, filed 12/3/2019. The date of 12/3/2019 is acknowledged.
Information Disclosure Statement
The IDS’s submitted on 4/6/2026 is under consideration.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Specifically, see Pg 26, lines 5-14; and Pg 38, lines 28-30 and 36.
Claim Objections
Claim 86 is objected to because of the following informality: The claim lists an amino acid sequence with 4 or more specifically defined and enumerated residues (Formula A) and therefore requires a SEQ ID NO. However, no SEQ ID NO is listed in the claim. See MPEP 2422 and 37 C.F.R. 1.821.
Claim 98 is objected to because of the following informality: There is a comma after “98” rather than a period, shown here:
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Appropriate correction is required.
Claim Interpretation
Claim 86 recites a GIP analogue consisting of Formula A, wherein X1 is selected from Glu, glutaric acid, succinic acid, and adipic acid or is omitted; Z is a peptide consisting of one or more consecutive amino acid residues of Extendin-4(31-39) or omitted; a fatty acid molecule is attached to a Lys residue at any position within Formula A or within Z if it is included; and the C-terminus is optionally amidated. Alternatively, the GIP analogue can be a functional variant, wherein said variant has 1-4 amino acid substitutions, with the exception that position 11 must be Aib and position 22 must be Glu; X1, Z, the fatty acid molecule attached to a Lys residue, and the optional C-terminal amidation are as described above. Functionally, the GIP analogue of Formula A or a functional variant thereof is an antagonist of GIPR.
Claim 87 recites the GIP analogue or functional variant of claim 1, wherein it possesses certain behaviors listed in (a)-(h). These limitations (a)-(h) describe functional rather than structural elements of the instant invention. As such, the claim is being interpreted based upon the structural limitation (a GIP analogue or functional variant thereof, described above) where the functional limitations (a)-(h) are properties endowed by the structure.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 86-91, 94-95, 97-99, 101-103, 107, and 109-114 are rejected under 35 U.S.C. 103 as being unpatentable over Just et al. (WO 2013164483 A1, published 11/7/2013) and Rosenkilde et al. (WO 2018/220123 A1, effectively filed 5/31/2017, cited on IDS filed 10/14/2025).
Just teaches truncated GIP analogues that comprise one or more substitutions as compared to wild-type GIP which may have the property of an altered, preferably increased GLP-1 activity (Abstract). Just teaches SEQ ID NO: 59/Formula I, which consists of:
R1-X1-X2-X3-Gly-Thr-Phe-X7-Ser-X9-X10-X11-Ile-X13-X14-X15-X16-X17-Ala-X19-X20-X21-X22-X23-X24-Trp-Leu-X27-X28-X39-X30-X31-X32-X33-X34-X35-X36-X37-X38-X39-X40-X41-X42-R2, wherein
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([0007]).
The above peptide wherein R1, X1, and X2 are any of the above; X3 is Glu; X7 is Ile; X9 is Glu; X10 is Tyr; X11 is Ser; X13 is Aib; X14 is Leu; X15 is Glu; X16 is Lys; X17 is Ile; X19 is Gln; X20 is Gln; X21 is Glu; X22 is Phe; X23 is Val; X24 is Glu; X27 is Leu; X28 is Ala; X29 is Gln; and X30 is Lys; X31 is Pro; X32 is Ser; X33 is Ser; X34 is Gly; X35 is Ala; X36-38 are Pro; X39 is Ser; X40-42 are absent; and R2 is either NH2 or OH reads upon the peptide sequence of Formula A of the instant claim 86, wherein X1 is Glu and Z is present.
Just further teaches that lipophilic substituents can be attached to one or more amino acid side chains, the addition of which is thought to bind to albumin in the bloodstream and shield the compounds from enzymatic degradation, thereby enhancing the half-life and modulating the potency of the compound ([0056]). The lipophilic substituent is comprised of 10-24 carbon atoms and includes an acyl group ([0060-0061]).
Just does not teach that the peptide consists of only residues X3-X30 with or without the Z peptide (equivalent to X1-X28 in the instant Formula A) nor that the amino acid at position X18 is Lys (equivalent to position 16 in the instant Formula A).
Rosenkilde teaches GIP-derived peptide analogues GIP(5-30) and GIP(3-30) which are antagonists of the GIP receptor, modified to comprise at least one fatty acid molecule to increase the molecule’s half-life while maintaining its antagonistic properties (Abstract). Rosenkilde teaches that introduction of Lys coupled to C16-diacid to position 18 (equivalent to position 16 in the instant Formula A) of GIP(3-30) results in a highly potent, long-acting GIP receptor antagonists (Figure 2; corresponding legend Pg 4; Table 1).
Thus, regarding claim 86, Just teaches a GIP analogue comprising the sequence R1-X1-X2-Glu-Gly-Thr-Phe-Ile-Ser-Glu-Tyr-Ser-Ile-Aib-Leu-Glu-Lys-Ile-Ala-Gln-Gln-Glu-Phe-Val-Glu-Trp-Leu-Leu-Ala-Gln-Lys; an optional C-terminal Z peptide consisting of PSSSGAPPPS; optional amidation of the C-terminus; and a lipophilic substituent attached to an amino acid side chain that improves the half-life and potency of the peptide. Rosenkilde teaches that removal of the first few amino acids from the N-terminus of GIP, resulting in GIP(3-30), produces GIP receptor antagonists; further, Rosenkilde indicates that modification of GIP(3-30) by substitution of His for Lys conjugated to a C16 fatty diacid further improves the half-life while maintaining the antagonistic properties of the peptide. Therefore, it would be prima facie obvious to truncate the peptide taught by Just, removing R1-X1-X2 from the sequence such that only residues 3-30 remained, in order to generate a GIP receptor antagonist. It would also be obvious to substitute the His residue at position 18 for Lys conjugated to a C16 fatty diacid to further improve the half-life and potency of the peptide antagonist, as taught by Rosenkilde. One would have a reasonable expectation of success in making these changes to the peptide taught by Just as Rosenkilde demonstrated that modifications improved the properties of GIP analogues over the wild-type GIP(3-30)-NH2.
Regarding claim 87, Table 3b of Rosenkilde indicates that the presence of Lys acylated at position 18 (equivalent to position 16 in the instant Formula A) results in IC50 values less than 10nM.
Regarding claim 88, as stated above, Rosenkilde teaches the attachment of fatty diacids, such as C16 fatty diacid, to Lys at position 18 (equivalent to position 16 the instant Formula A).
Regarding claim 89, Rosenkilde teaches that position 11 (equivalent to position 9) can be K; position 14 (equivalent to position 12) can be M, L, or Nle; position 15 (equivalent to position 13) can be D or E; position 16 (equivalent to position 14 in the instant Formula A) can be K or R; position 18 (equivalent to position 16) can be H or K; and conservative substitutions are also contemplated (Pg 24-25).
Regarding claims 90 and 102, Rosenkilde teaches that GIP peptide analogues can have 1-6 amino acid substitutions (Pg 17, line 32 – Pg 18, line 2).
Regarding claim 91, Rosenkilde teaches amino acid substitutions (see above regarding claim 89) that are not at positions 7 and/or 19. Additional substitutions at other positions beyond the instant position 13 are also contemplated by Rosenkilde (Pg 24-25).
Regarding claim 94, as stated above, Just teaches that the Z peptide can consist of PSSGAPPPS (the instant SEQ ID NO: 67). Just also teaches GPSSGAPPPS (instant SEQ ID NO: 61)) ([0025]).
Regarding claim 95, as stated above, Rosenkilde teaches the substitution of His for Lys conjugated to C16 fatty diacid at position 18 (equivalent to position 16 in the instant Formula A).
Regarding claim 97, as stated above, Just and Rosenkilde teach a peptide consisting of the sequence Glu-Gly-Thr-Phe-Ile-Ser-Glu-Tyr-Ser-Ile-Aib-Leu-Glu-Lys-Ile-Lys-Gln-Gln-Glu-Phe-Val-Glu-Trp-Leu-Leu-Ala-Gln-Lys-Z, wherein Z is PSSSGAPPPS (SEQ ID NO: 79).
Regarding claim 98, as stated above, Just teaches that the C-terminus can be a free carboxylic acid.
Regarding claim 99, Rosenkilde teaches that the fatty acid molecule can be a straight-chain fatty acid, a branched fatty acid, a monoacyl fatty acid, a diacyl fatty acid, an acyl group of the formula CH3(CH2)nCO- wherein n is an integer from 4-24, or an acyl group selected from CH3(CH2)14CO-, CH3(CH2)16CO-, CH3(CH2)18CO-, CH3(CH2)20CO- (Pg 41, line 31 – Pg 42, line 17).
Regarding claims 101 and 103, as stated above, Just and Rosenkilde teach the elected species EGTFISEYSIAibLEKIKQQEFVEWLLAQKPSSSGAPPPS, wherein a C16 fatty diacid is attached to the Lys at position 16 of Formula A (SEQ ID NO: 18 C16-diacid/16K).
Regarding claim 107, as stated above, Just teaches the addition of the Z peptide consisting of PSSGAPPPS (SEQ ID NO: 61) to the C-terminus ([0007]).
Regarding claim 109-114, Just teaches that peptides of the invention can be formulated as acid addition salts, which can include hydrochloride salts and sodium salts ([0084]).
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 filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual 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/apply/applying-online/eterminal-disclaimer.
Claim 86-91, 97-99, 101-103, 107 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 and 11-17 of U.S. Patent No. 12,297,250 B2 (US ‘250). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘250 recites a GIP analogue consisting of the amino acid sequence SEQ ID NO: 81:
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wherein said amino acid sequence is modified by attaching a fatty acid molecule at one or more amino acid residues, directly or via a linker, at any one of positions 3-29 of SEQ ID NO: 81, wherein Z is a peptide of one or more amino acid residues of GIP(31-42) (GKKNDWKHNITQ; SEQ ID NO: 2) or wherein Z is a peptide of one or more amino acid residues of Extendin-4 (HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS; SEQ ID NO: 3), wherein said amino acid sequence is optionally C-terminally amidated (-NH2) or C-terminally carboxylated (-COOH), and wherein said GIP analogue is an antagonist of GIPR.
Dependent claims include functional attributes of the GIP analogue (claim 2), the identity of the Z polypeptide (claims 3 and 4), the position and residue that the fatty acid molecule is attached to (claims 5 and 6), the C-terminal modification (claim 7), the identity of the fatty acid (claims 8 and 9), species of the above SEQ ID NO: 81 (claims 11-14), methods of treating obesity comprising administering the GIP analogues (claims 15-17; the instant specification notes that claimed peptides of the invention can be used to treat obesity, for example, on Pg 4, lines 32-33).
Claims 86-91, 94-95, 97-99, 101-103, 107 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 112-113, 119-125, 128, 129, and 131 of copending Application No. 18/565,984 (‘984, reference application; claims filed 7/9/2024). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 112 of copending Application No. ‘984 recites a method for treatment of obesity, an obesity-related disorder and/or dyslipidemia, said method comprising administration to an individual in need thereof a therapeutically effective amount of a glucagon-like peptide-1 (GLP-1) receptor agonist and a therapeutically effective amount of a glucose-dependent insulinotropic peptide receptor (GIPR) antagonist GIP peptide, said GIP peptide consisting of the amino acid sequence SEQ ID NO:1:
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wherein X1 is E, glutaric acid, adipic acid or succinic acid; wherein X2 is M, L or Nle; or a functional variant thereof, wherein said variant has 1, 2 or 3 individual amino acid substitutions at any amino acid residue of SEQ ID NO: 1, wherein said GIP peptide comprises a fatty acid molecule attached, directly or via a linker, to the side chain amino group of the amino acid residue at position 18 of SEQ ID NO:1, or said functional variant thereof. This reads on the instant Formula A of claim 86, wherein X1 is E, gluartic acid, adipic acid, or succinic acid and X2 is L or Nle and Z of the instant Formula A is included. Claim 113 of copending Application No. ‘984 recites a similar method for inhibiting food intake, body weight, fasting blood levels of glucose, fasting blood levels of insulin, insulin resistance, fasting blood levels of triglycerides, fasting blood levels of cholesterol, and fasting blood levels of LDL cholesterol, comprising administration to an individual in need thereof a therapeutically effective amount of a GLP-1 receptor agonist and a therapeutically effective amount of a GIPR antagonist GIP peptide, which consist of the above amino acid sequence.
The instant specification indicates that the instant peptides of the invention can be used to treat obesity, obesity-related disorders, and dyslipidemia (Pg 4, line 32, - Pg 5, line 4).
Dependent claims include further limitations regarding additional species (claims 119-120, 125, 128, 129), fatty acid molecule attachment (claims 122-124), C-terminal modifications (claim 121), species of the obesity-related disorder (claim 126; the instant specification indicates such species can be treated with peptides, see, for instance, Pg 59, lines 5-19), and a kit thereof (claim 131).
Claims 86-91, 94-95, 97-99, 101-103, 107 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims of copending Application No. 19/096,393 (‘393, reference application; claims filed 8/28/2025). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 99 of copending Application No. ‘393 recites a glucose-dependent insulinotropic peptide (GIP) analogue comprising the amino acid sequence of Formula A:
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or a functional variant thereof, wherein the amino acid positions of Formula A are numbered in accordance with the amino acid sequence of native GIP(1-42), wherein said variant has 1-4 individual amino acid substitutions at any amino acid residue of SEQ ID NO: 174, wherein a fatty molecule is attached, directly or via a linker, to an amino acid residue of SEQ ID NO : 174, or said functional variant thereof, wherein said amino acid sequence is optionally C-terminally amidated (-NH2) or C-terminally carboxylated (-COOH), and wherein said GIP analogue is an antagonist of GIPR. This reads on Formula A of the instant claim 86.
Dependent claims include further limitations regarding GIP peptide analogue antagonistic function (claim 100), amino acid substitutions (claims 101, 102, 103, 104), species of SEQ ID NO: 174 (claims 105, 106, 115, 116, , 17, 118), fatty acid molecule attachment (claims 107-110, 112-113), the C-terminal modifications (claim 111), and a method of treating a condition related to obesity, pre-diabetes, insulin resistance, elevated fasting glucose, and hyperglycemia (claim 119; the instant specification indicates such species can be treated with peptides, see, for instance, Pg 59, lines 5-19).
Conclusion
No claim is 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 nonprovisional extension fee (37 CFR 1.17(a)) 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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sara Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa L Fisher can be reached at 571-270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
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