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Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn.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, see Pg 20-27, filed 10/14/2025, with respect to the rejection(s) of claim(s) 86-99 and 101-103 under 35 U.S.C. 103 have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection is made in view of the amended claims.
Applicant’s arguments that substitution of A11Aib and N22E confers unexpected improvements to the claimed GIP analogues is noted. Unexpected results must be compared to the closest prior art, which is Sparre-Ulrich (US20220298218 A1, effectively filed 12/3/2018, cited on IDS filed 10/14/2025) cited in a new art rejection below. Sparre-Ulrich anticipates the instant claims, meaning that these results are not unexpected. Further, the claims are rendered obvious by Just et al. (WO 2013164483 A1, published 11/7/2013) in view of Rosenkilde et al. (WO 2018/220123 A1, effectively filed 5/31/2017, cited on IDS filed 10/14/2025), also cited in a new art rejection below. Thus, the argument that the results are unexpected results is not persuasive.
Applicant’s request that the double patenting rejections be held in abeyance is noted but they have been modified and maintained 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 86-91, 95, 97-99, 101, and 103 are currently amended. Claims 94 and 102 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 Claims 100, 104-106, and 108 are withdrawn as non-elected species (claims 100, 104, 105, and 108) and inventions (claim 106). Claims 107-114 are new.
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 2/7/2025 and 10/14/2025 are under consideration.
The previous Office Action incorrectly indicated that the IDS filed 2/7/2025 failed to comply with the provisions of 37 CFR 1.98(a)(4) because it lacked the appropriate size fee assertion. This objection is herein withdrawn and the contents of the IDS filed 2/7/2025 are under consideration.
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 95 is objected to because of the following informality: in line 3, where the amino acid positions 9, 10, 11, 14, 15, 16, and 18 are listed, include and “or” between “position 16” and “position 18” such that the claim reads “position 16, or position 18” (emphasis added) for improved readability.
Appropriate correction is required.
Claim Interpretation
Claim 1 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 2 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 § 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 88, 95, 97, 101, 103, and 112 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.
Claim 88 recites that the fatty acid molecule can be attached to one lysine residue at any one of positions 1-27 or 2-27 of Formula A. The scope of this claim is indefinite because it is unclear whether the fatty acid attached to the lysine residue an occupy position 1 or not. For purposes of examination, the claim is being interpreted as the fatty acid attached to the lysine residue can occupy any position 1-27 of Formula A.
Claim 95 recites that the fatty acid molecule is attached to the side chain of Lys amino acid residue at positions 9, 10, 11, 14, 15, 16, or 18 or at positions 10, 11, 14, 15, and 16, or at position 16. The scope of this claim is indefinite as it is unclear whether the fatty acid molecule can only be attached to the Lys at position 16, as stated in the narrowest limitation, or whether it can occupy any of the positions 9, 10, 11, 14, 15, 16, or 18 as in the broadest limitation. For purposes of examination, the claim is being interpreted as the fatty acid attached to the lysine can occupy any position of 9, 10, 11, 14, 15, 16, or 18.
Claims 97, 101, and 103 all depend from claim 86, which indicates that the GIP analogue consists of Formula A or a functional variant thereof that has 1-4 amino acid substitutions at any amino acid except for positions 11 and 22 which must be occupied by Aib and E, respectively. Claims 97, 101, and 103 all subsequently recite species of Formula A in terms of SEQ ID NO, but further include a functional variant limitation wherein the functional variant has 1-4 amino acid substitutions (or, in the case of claim 103, 1-2 amino acid substitutions) except for Aib at position 11 and Glu at position 22. The scope of these claims is indefinite as it is unclear whether the additional 1-4 or 1-2 amino acid substitutions recited in the claims are in addition to those recited in claim 86 or collectively only 1-4 or 1-2 amino acid substitutions should be made relative to Formula A as recited in claim 86. Additionally, because it depends from claim 101, claim 112 is also hereby rejected for this same reasoning. For purposes of examination, the claims are being interpreted as 1-4 amino acid substitutions in total may be made relative to Formula A except for positions 11 and 22.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 91 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 91 recites that the amino acid residue at position 7, 13, and/or 19 of Formula A is E. This does not further limit the parent claim, claim 86, because in Formula A each of those positions 7, 13, and 19 is already E.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 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 –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 86-91, 94-95, 97-98, 99, 101-103, 107, and 109-114 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Sparre-Ulrich (US20220298218 A1, effectively filed 12/3/2018, cited on IDS filed 10/14/2025), as evidenced by Gupta et al. (Salts of Therapeutic Agents: Chemical, Physicochemical, and Biological Considerations. Molecules. 2018 Jul 14;23(7):1719.).
The applied reference has a common assignee and/or joint inventor with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed in the reference and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement.
Sparre-Ulrich teaches GIP-derived peptide analogues that are antagonists of the GIP receptor (Abstract). One such peptide taught by Sparre-Ulrich is SEQ ID NO: 81, shown below:
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, which meets the limitations of Formula A of the instant claim 86, wherein X1 = E, position 11 is Aib, position 22 is Glu, and Z is omitted.
Sparre-Ulrich also teaches SEQ ID NO: 174:
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which consists of SEQ ID NO: 81 in addition to the C-terminal Z polypeptide, wherein Z consists of PSSGAPPPS.
Additional species of SEQ ID NO: 174 are also taught, such as “AT673” which has the sequence EGTFISEYSIAibLEKIKQQEFVEWLLAQKPSSGAPPPS-C16-diacid/18K, wherein a C16 fatty diacid is attached to the Lys at position 18 (equivalent to position 16 in the instant Formula A; very bottom of Pg 29); this species is identical to the elected SEQ ID NO: 18 C16-diacid/16K. Thus, claim 86 is anticipated.
Sparre-Ulrich teach that peptides of the invention can inhibit GIPR activity at least 70% based on measured changes in intracellular cAMP ([0539-0540]). Additionally, the antagonistic activity corresponds to an IC50 of 10nM or less ([0541]); the peptides have increased physical stability, including increased solubility ([0773]; also see of Table 1C). Thus, claim 87 is anticipated.
The peptide AT673 includes a Lys attached to a fatty acid at position 18 (equivalent to position 16 in the instant Formula A). Thus, claim 88 is anticipated.
Sparre-Ulrich teaches other GIP analogue functional variants that comprise substitutions such as D, E, and T at position 9 (equivalent to position 7 in the instant Formula A); S, K, and A at position 11 (equivalent to position 9); I, K, and Aib at position 12 (equivalent to position 10); A or Aib at position 13 (equivalent to position 11); M, K, E, S, L, and Nle at position 14 (equivalent to position 12); D and E at position 15 (equivalent to position 13); K and R at position 16 (equivalent to position 14); I and K at position 17 (equivalent to position 15); H and K at position 18 (equivalent to position 16); Q and K at position 20 (equivalent to position 18); and D and E at position 21 (equivalent to position 19) ([0101-0111]).
Sparre-Ulrich also teach functional variants of the aforementioned peptides, such as those with 1-4 amino acid substitutions. Thus, claims 90 and 102 are anticipated.
In the peptide AT673, Glu occupies positions 9, 15, and 21 (equivalent to positions 7, 13, and 19 in the instant Formula A). Moreover, a Lys occupies position 18 (equivalent to position 16 in the instant Formula A). Thus, claims 91 and 95 are anticipated.
Sparre-Ulrich further teaches that the C-terminal Z peptide can be selected from a glycine or a proline, a fragment selected from SEQ ID NO: 4-16 or a variant thereof comprising 1 or 2 individual amino acid substitutions ([0038-0085; 0087; 0089]. Thus, claims 94 and 107 are anticipated.
The aforementioned SEQ ID NO: 81 anticipates the instant SEQ ID NO: 79. SEQ ID NO: 81 also has a free C-terminal carboxylic acid. Thus, claims 97 and 98 are anticipated.
Sparre-Ulrich further 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 to 24; or selected from the group consisting of CH3(CH2)14CO-, CH3(CH2)16CO-, CH3(CH2)18CO-, or CH3(CH2)20CO- ([0390-0392, 0394, 0396-0401]. Thus, claim 99 is anticipated.
As stated above, AT673, which has the sequence EGTFISEYSIAibLEKIKQQEFVEWLLAQKPSSGAPPPS-C16-diacid/18K, wherein a C16 fatty diacid is attached to the Lys at position 18 (equivalent to position 16 in the instant Formula A; very bottom of Pg 29) anticipates the elected species SEQ ID NO: 18 C16-diacid/16K. Thus, claim 101 and 103 are anticipated.
Sparre-Ulrich further teaches acid addition salts of the peptides of the invention ([0700]), thus anticipating claim 109.
Sparre-Ulrich also teaches that peptides of the invention can be formulated as pharmaceutically acceptable salts. As evidenced by Gupta et al., common examples of couterions for salt formation include both sodium and chloride (Table 1). Thus, claims 110-114 are anticipated.
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, 97-98, 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 modulate 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 and 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 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 claims 89 and 91, Rosenkilde teaches that K can be D, E, S, R and A at position 16 (equivalent to position 14 in the instant Formula A); M can be L, S, K, Nle, or Mox at position 14 (equivalent to position 12); D can be E, A, Orn, or K at position 15 (equivalent to position 13); H can be A, R, Orn, or K at position 18 (equivalent to position 16); S can be Orn or K at position 11 (equivalent to position 9); 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 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.
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.
Regarding claim 107, as stated above, Just teaches the addition of the Z peptide consisting of PSSGAPPPS 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.
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/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/FRED H REYNOLDS/Primary Examiner, Art Unit 1658