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 .
DETAILED ACTION
Election/Restriction
REQUIREMENT FOR UNITY OF INVENTION
As provided in 37 CFR 1.475(a), a national stage application shall relate to one invention only or to a group of inventions so linked as to form a single general inventive concept (“requirement of unity of invention”). Where a group of inventions is claimed in a national stage application, the requirement of unity of invention shall be fulfilled only when there is a technical relationship among those inventions involving one or more of the same or corresponding special technical features. The expression “special technical features” shall mean those technical features that define a contribution which each of the claimed inventions, considered as a whole, makes over the prior art.
The determination whether a group of inventions is so linked as to form a single general inventive concept shall be made without regard to whether the inventions are claimed in separate claims or as alternatives within a single claim. See 37 CFR 1.475(e).
When Claims Are Directed to Multiple Categories of Inventions:
As provided in 37 CFR 1.475 (b), a national stage application containing claims to different categories of invention will be considered to have unity of invention if the claims are drawn only to one of the following combinations of categories:
(1) A product and a process specially adapted for the manufacture of said product; or
(2) A product and a process of use of said product; or
(3) A product, a process specially adapted for the manufacture of the said product, and a use of the said product; or
(4) A process and an apparatus or means specifically designed for carrying out the said process; or
(5) A product, a process specially adapted for the manufacture of the said product, and an apparatus or means specifically designed for carrying out the said process.
Otherwise, unity of invention might not be present. See 37 CFR 1.475 (c).
Restriction is required under 35 U.S.C. 121 and 372.
This application contains the following inventions or groups of inventions which are not so linked as to form a single general inventive concept under PCT Rule 13.1.
In accordance with 37 CFR 1.499, applicant is required, in reply to this action, to elect a single invention to which the claims must be restricted.
Group I, claim(s) 1-11, drawn to a hybrid peptide and its pharmaceutical composition.
Group II, claim(s) 12-16, drawn to a method of administering the hybrid peptide of Group I to treat a disease or condition .
This application contains claims directed to more than one species of the generic invention. These species are deemed to lack unity of invention because they are not so linked as to form a single general inventive concept under PCT Rule 13.1.
The species are as follows:
Genus P: (Peptide , claims 9-10)
Elect a single polypeptide SEQ ID NO listed in claims 9-10.
Genus K*: (claim 6)
Lys-g-Glu-g-Glu-C=O(CH2)18CO2H,
Lys-γ-Glu-γ-Glu-C=O(CH2)18CH3,
Lys(AEEAcAEEAc-γ-Glu-19-carboxynonadecanoyl,
Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl
Genus D: (Disease in claim 12)
Obesity
Metabolic disease
Liver disorder
The groups of inventions listed above do not relate to a single general inventive concept under PCT Rule 13.1 because, under PCT Rule 13.2, they lack the same or corresponding special technical features for the following reasons:
Groups I-II lack unity of invention because even though the inventions of these groups require the technical feature of a hybrid GIP polypeptide, this technical feature is not a special technical feature as it does not make a contribution over the prior art in view of Levy et al. (WO2006/086769 A2, cited in IDS) in view of Gabe et al. (Peptides. 2020 Mar:125:170224) and Mahalakshmi et al. (Methods Mol Biol. 2006:340:71-94).
Levy et al. teach a GIP hybrid polypeptide comprising an N-terminal GIP analog fragment in combination with a C-terminal polypeptide having glucose lowering activity [0020].
Levy et al. teach the GIP analog domain consisting of YA2EGTFI7SDYSIA13M14 [00293] and further teach alanine can be modified by 4-amino butyric amino acid (Aib) to resist DPP-IV at position 2 [0079, last line to 0080]. Levy et al. further teach substitutions of Met14 to Leu and His18 to Ala [0083, 00288]. Levy et al. further show substitution of Ile7 to Thr in various GIP analog polypeptide sequences [0084]. Levy et al. show a table for amino acid substitution of generating a GIP analog peptide comprising (i) Leu to ala (reading on Leu 21 to Ala), (ii) Leu to ile (reading Leu 27 to Ile), and (iii) Asn to gln (reading on Asn 24 to Gln) [00330 and 00297-0029]. Although Levy et al. did not specify further substitution of A13 to Aib, Gabe et al. show GIP folded as a helical protein bound to the GIP receptor (p3, Fig 3). Mahalakshmi et al. teach α-amino-isobutyric acid (Aib) and related Cαα dialkylated residues are strong promoters of helix formation (Summary). Mahalakshmi et al. teach centrally positioned Aib residues can promote formation of an incipient 310 helix by recruiting both the preceding and succeeding residues to the formation of a consecutive type III β-turn structure (p77, Sec 2.2. Helices). Because (i) Levy et al. teach ala can be substituted by Aib in a GIP analog peptide [00276], (ii) Gabe et al. show GIP forming a helical structure bound to its receptor and (iii) Mahalakshmi et al. teach centrally positioned Aib residues can promote formation of an incipient 310 helix, one of ordinary skill in the art would have found it obvious to beneficially substitute A13 of Levy’s GIP to Aib. Levy et al. further teach a GIP hybridized to a peptide consisting of the following sequence “KCNTATCVLGRLSQELHRLQTYPRTNTGSNTY” preferably in its C-terminal amide form [00238]. Levy et al. teach the amino acids the of last four amino acids at the C-terminus of GIP are X27= I, X28=A, and X29-30 as GG [00297-00299]. Levy’s GIP analog peptide
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compared to the claimed SEQ ID NO: 15 as follows shows the only difference is the linker sequence according the instant peptide formula (I). Levy et al. further teach a Trp-cage peptide sequence of PSSGAPPPS can be further added to the C-terminus of the modified GIP [0035] to connect the second hormone peptide, reading on the peptide SEQ ID NO: 15 (K* = lysine) in claims 1 and 9. Since the technical feature was known in the art, this instant invention lacks unity of invention without a special technical feature.
During a telephone conversation with Mr. Dean L. Fanelli on 1/8/2026 a provisional election was made without traverse to prosecute the invention of Group I, claims 1-11. Affirmation of this election must be made by applicant in replying to this Office action. Claims 12-16 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention. In response to species election, applicant’s representative elected the peptide sequence of SEQ ID NO: 40 and Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl), reading on claims 1, 6, 9, and 11.
Applicant is reminded that upon the cancelation of claims to a non-elected invention, the inventorship must be corrected in compliance with 37 CFR 1.48(a) if one or more of the currently named inventors is no longer an inventor of at least one claim remaining in the application. A request to correct inventorship under 37 CFR 1.48(a) must be accompanied by an application data sheet in accordance with 37 CFR 1.76 that identifies each inventor by his or her legal name and by the processing fee required under 37 CFR 1.17(i).
The examiner has required restriction between product or apparatus claims and process claims. Where applicant elects claims directed to the product/apparatus, and all product/apparatus claims are subsequently found allowable, withdrawn process claims that include all the limitations of the allowable product/apparatus claims should be considered for rejoinder. All claims directed to a nonelected process invention must include all the limitations of an allowable product/apparatus claim for that process invention to be rejoined.
In the event of rejoinder, the requirement for restriction between the product/apparatus claims and the rejoined process claims will be withdrawn, and the rejoined process claims will be fully examined for patentability in accordance with 37 CFR 1.104. Thus, to be allowable, the rejoined claims must meet all criteria for patentability including the requirements of 35 U.S.C. 101, 102, 103 and 112. Until all claims to the elected product/apparatus are found allowable, an otherwise proper restriction requirement between product/apparatus claims and process claims may be maintained. Withdrawn process claims that are not commensurate in scope with an allowable product/apparatus claim will not be rejoined. See MPEP § 821.04. Additionally, in order for rejoinder to occur, applicant is advised that the process claims should be amended during prosecution to require the limitations of the product/apparatus claims. Failure to do so may result in no rejoinder. Further, note that the prohibition against double patenting rejections of 35 U.S.C. 121 does not apply where the restriction requirement is withdrawn by the examiner before the patent issues. See MPEP § 804.01.
The office action of examination is in the following page.
DETAILED ACTION
Election/Restrictions
Applicant’s election without traverse of Group (I), claims 1-11, by phone on 1/8/2026 is acknowledged.
In response to the species election, applicant elected SEQ ID NO: 40 conjugated with Lys(AEEAc-AEEAc-y-Glu-17-carboxyheptadecanoyl).
Claim Status
Claims 1-16 are pending.
Claims 12-16 are withdrawn as being directed to a non-elected invention, the election having been made on 1/8/2026. In response to species election, applicant elected the peptide SEQ ID NO: 40 conjugated with Lys(AEEAc-AEEAc-y-Glu-17-carboxyheptadecanoyl) at X9 position; thus, claims 2-5, 7-8, and 10 NOT reading on the elected species of SEQ ID NO: 40 conjugate are further withdrawn.
Claims 1, 6, 9, and 11 have been examined.
Priority
This application has PRO 63/435,723 12/28/2022
This application has PRO 63/389,769 07/15/2022
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 12/8/2023, 2/2/2024, 4/4/2024, and 7/10/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Sequence Compliance
The amino acid sequence disclosure contained in this application does not comply with the requirements for such a disclosure as set forth in 37 C.F.R.1.821-1.825. At least the peptide sequences found in the SPEC [0028, 00134, 00278, 00403, 00426, 00455, 00490, 00652, 00747, 00953-00954] and in claim 1 require SEQ ID NOs. See PTO-2301 attached in details.
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Specification
The specification is objected to because the peptide sequences in the paragraph [0028, 00134, 00278, 00403, 00426, 00455, 00490, 00652, 00747, 00953-00954] require SEQ ID Nos.
Claim Objections
Claims 1 and 9 are objected to because of the following informalities:
Claim 1 is object to due to missing a SEQ ID NO for the peptide formula (I).
Claim 1 is further object to because the definition of “X7 is G, is Gln, …” should be revised to “X7 is G, Gln, …” by deleting the extra underlined word “is”.
Claim 9 is object to because of the format of “SEQ. ID. NO.” in the table should be revised to “SEQ ID NO:”. Each claim should have a single period “.” at the end of the claim.
Appropriate correction is required.
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.
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.
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.
1. Claims 1, 9, and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Levy et al. (WO2006/086769 A2, cited in IDS) in view of Gabe et al. (Peptides. 2020 Mar:125:170224), Mahalakshmi et al. (Methods Mol Biol. 2006:340:71-94).
Claim 1 is drawn to a peptide formula (I).
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Levy et al. teach a GIP hybrid polypeptide comprising an N-terminal GIP analog fragment in combination with a C-terminal polypeptide having glucose lowering activity [0020]. Levy et al. teach the functional motifs of GIP hybrid polypeptide can be described as D-L-C-S defined as follows [00264].
Levy et al. teach the domain consisting of YA2EGTFI7SDYSIA13M14 [00293] and further teach alanine can be modified by 4-amino butyric amino acid (Aib) to resist DPP-IV at position 2 [0079, last line to 0080]. Levy et al. further teach substitutions of Met14 to Leu and His18 to Ala [0083, 00288]. Levy et al. further show substitution of Ile7 to Thr in various GIP analog polypeptide sequences [0084]. Levy et al. show a table for amino acid substitution of generating a GIP analog peptide comprising (i) Leu to ala (reading on Leu 21 to Ala), (ii) Leu to ile (reading Leu 27 to Ile), and (iii) Asn to gln (reading on Asn 24 to Gln) [00330 and 00297-0029].
Levy et al. did not specify further substitution of A13 to Aib.
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Gabe et al. show GIP folded as a helical protein bound to the GIP receptor as follows (p3, Fig 3). Mahalakshmi et al. teach α-amino-isobutyric acid (Aib) and related Cαα dialkylated residues are strong promoters of helix formation (Summary). Mahalakshmi et al. teach centrally positioned Aib residues can promote formation of an incipient 310 helix by recruiting both the preceding and succeeding residues to the formation of a consecutive type III β-turn structure (p77, Sec 2.2. Helices). Because (i) Levy et al. teach ala can be substituted by Aib in a GIP analog peptide [00276], (ii) Gabe et al. show GIP forming a helical structure bound to its receptor and (iii) Mahalakshmi et al. teach centrally positioned Aib residues can promote formation of an incipient 310 helix, one of ordinary skill in the art would have found it obvious to beneficially substitute the centrally positioned A13 in Levy’s GIP to Aib. Levy et al. further teach a GIP hybridized to a peptide consisting of the following sequence of “KCNTATCVLGRLSQELHRLQTYPRTNTGSNTY” preferably in its C-terminal amide form [00238]. Levy et al. teach the amino acids the of last four amino acids at the C-terminus of GIP are X27= I, X28=A, and X29-30 as GG [00297-00299]. When, Levy’s GIP analog peptide compared to the claimed SEQ ID NO: 15 as follows shows the only difference is the linker sequence according the instant peptide formula (I). Levy et al. further teach a Trp-cage peptide sequence of PSSGAPPPS can be further added to the C-terminus of the modified GIP [0035] to link the second hormone peptide as follows, reading on the peptide SEQ ID NO: 15 (K* = lysine) in claims 1 and 9.
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With respect to claim 11, Levy et al. teach a pharmaceutical composition comprising the GIP hybrid polypeptide (e.g., SEQ ID NO: 15) and a pharmaceutically acceptable carrier [00353] such as buffer solution with salts [00473].
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Levy et al. with (ii) Gabe et al. in view of Mahalakshmi et al. because (a) Levy et al. teach a modified GIP hybrid peptide comprising Ala substituted by Aib [00276], (b) Gabe et al. show GIP forming a helical structure bound to its receptor (p3, Fig 3), and (c) Mahalakshmi et al. teach centrally positioned Aib residues can beneficially promote formation of an incipient 310 helix (p77, Sec 2.2. Helices). The combination would have reasonable expectation of success because centrally positioned Ala18 in GIP substituted by Aib is expected to promote helical protein structure as taught by Mahalakshmi et al.
2. Claims 1, 6, 9, and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Levy et al. in view of Gabe et al., Mahalakshmi et al. as applied to claims 1, 9, 11, and further in view of Musaimi et al. (2017 FDA PEPTIDE HARVEST, Spain, 2018)
Claim 6 is drawn to GIP hybrid peptide conjugated with fatty acid moiety at a lysine residue including the elected species of Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl).
Levy et al. teach the GIP hybrid peptide conjugated to fatty acid via a lysine residue [00303] and the GIP hybrid peptide consists of a single lysine residue corresponding to the X9 position of the peptide formula (I) as applied to claims 1, 9, and 11, but did not specify the conjugated lysine as Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl).
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Similarly, Musaimi et al. teach fatty acid conjugated to GLP-1 analog peptide via Glu residue linked to the Lys side-chain through the γ -carboxylic group to generate Semaglutide shown as follows (page 5). Because both Levy et al. and Musaimi et al. teach fatty acid conjugate to a lysine residue of a therapeutic peptide, one of ordinary skill in the art would have found it obvious to conjugate a fatty acid to Levy’s GIP hybrid peptide via Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl) as taught by Musaimi et al., reading on the elected conjugation species in claim 6.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Levy et al. in view of Gabe et al. and Mahalakshmi et al. with (ii) Musaimi et al. because (a) Levy et al. teach the GIP hybrid peptide conjugated to fatty acid via a lysine residue [00303], (b) Musaimi et al. show fatty acid conjugated to GLP-1 analog peptide via Glu residue linked to the Lys side-chain through the γ -carboxylic group for a therapeutic polypeptide (page 5). The combination would have reasonable expectation of success because both Levy et al. and Musaimi et al. teach conjugation of a fatty acid derivative to a lysine side chain of a peptide.
3. Claims 1, 6, 9, and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Levy et al. in view of Gabe et al., Mahalakshmi et al., Musaimi et al. as applied to claims 1, 6, 9, 11, and further in view of Ryge et al. (US 2010/0048462 A1).
Claim 9 is drawn to the elected peptide sequence of SEQ ID NO: 40.
Levy et al. teach GIP analog peptide can be linked to a second hormone module/peptide via directly linked by the carboxy of a first module to the amino of a second module (reading on an amide bond). In addition, Levy et al. further teach any linking moiety can be used to attach the modules/peptides known in the art including PEG; amino acid, e.g., Lys, Glu, beta-Ala; polyaminoacids; bi-functional linkers, cleavable or non -cleavable linker. Levy et al. teach a glycine linker 1 to 30 residues in length [00217] or beta alanine linker [00337] in addition to a linker of PSSGAPPPS or its modified linker of PSSG [00305], consistent with this instant disclosure in the specification that the peptide domains in a GIP hybrid polypeptide can be connected either directly or via a linker [00245, 00274-PEG, 00863-Trp Cage, 00915-glycine or other peptide linker)]. Levy et al. teach the amino acids of the last four amino acids at the C-terminus of GIP of X27-30 are optional [00297-00299]. When X28=A and X29-30 = absent with a linker PSSG or GGGG, various Levy’s GIP hybrid polypeptide compared to the elected SEQ ID NO: 40 show the difference among the polypeptides is the linker/spacer sequence of GGPS as
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follows.
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Ryge et al. is cited to show conservative substitution of amino acids among Gly, Ser, and Pro with same physicochemical properties in a peptide known to one of ordinary skill in the art shown as follows [0075, Table 2].
Because (a) applicant admits GIP hybrid polypeptide can be connected either directly or via a linker in the specification [00245, 00274-PEG, 00863-Trp Cage, 00915-glycine or other peptide linker], consistent with Levy’s teaching described above, (b) Levy’s glycine linker or modified linker of PSSG are expected to connect the modified GIP* peptides in various length to the other hormone peptide to control plasma levels and/or treat various diseases/conditions taught by Levy et al. in the Abstract, and (c) Ryge et al. show conservative substitution of amino acids among Gly, Ser, and Pro with same physicochemical properties in a peptide known to one of ordinary skill in the art [0075, Table 2], one of ordinary kill in the art would recognize Levy’s GIP hybrid polypeptide comprising functionally equivalent peptide linkers (e.g., GGGG, PSSG) obvious to the instant linker of GGPS with the same physicochemical properties in the SEQ ID NO: 40. Thus, the elected peptide species of SEQ ID NO: 40 is further rejected by Levy et al. in view of Gabe et al., Mahalakshmi et al., Musaimi et al. and Ryge et al.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Levy et al. in view of Gabe et al., Mahalakshmi et al. and Musaimi et al. with (ii) Ryge’s conservative substitutions of amino acids for creating analog peptides because (a) Levy et al. in view of Gabe et al., Mahalakshmi et al. and Musaimi et al. teach a GIP hybrid with a poly glycine or a linker comprising a mixture amino acids of G, S, and P linker to connect the functional peptide domains and (b) Ryge et al. teach conservative substitutions among Gly, Ser, and Pro with same physicochemical properties for creating analog peptides.
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.
Claims 1, 6, 9, and 11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 17/812,993 (the ‘993 application dated 7/2/2025) in view of Levy et al. (WO2006/086769 A2), Gabe et al. (Peptides. 2020 Mar:125:170224), Mahalakshmi et al. (Methods Mol Biol. 2006:340:71-94), Musaimi et al. (2017 FDA PEPTIDE HARVEST, Spain, 2018) and evidenced by Rondinone et al. (US 2023/0203100 A1).
Claim 1 of the ‘993 application disclosed a GIP hybrid polypeptide comprising a modified GIP analog (underlined from X1 to X11) linked to a second functional peptide via a tetrapeptide linker X12-X15 (reading on GGPS) shown as follows.
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Claim 1 of the ‘993 application further disclosed a fatty acid derivative conjugated to a lysine side chain of the GIP hybrid peptide.
The relevancy of Levy et al. in view of Gabe et al., Mahalakshmi et al., Musaimi et al. and evidenced by Rondinone et al. as applied to claims 1, 6, 9, and 11 described above not repeated here.
Because Levy et al. in view of Gabe et al., Mahalakshmi et al., Musaimi et al. teach beneficial conjugation of a fatty acid derivative to a modified GIP hybrid polypeptide, GIP(1-28) analog peptide-(linker)-“KCNTATCVLGRLSQELHRLQTYPRTNTGSNTY” shown in the excel table above, via the lysine side chain of Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl), one of ordinary skill in the art would have found it obvious to conjugate the same peptide hormone to the GIP analog peptide taught by claim 1 of the ‘993 application via a linker GGPS (X12-X15) taught by claim 1 of the ‘993 application to produce the elected peptide species of SEQ ID NO: 40.
Thus, claim 1 of the ‘993 application in view of Levy et al., Gabe et al., Mahalakshmi et al., Musaimi et al. and evidenced by Rondinone et al. are obvious to the instant claims 1, 6, 9, and 11.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JIA-HAI LEE whose telephone number is (571)270-1691. The examiner can normally be reached Mon-Fri from 9:00 AM to 6:00 PM.
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/J.L/Examiner, Art Unit 1658
04-February-2026
/LI N KOMATSU/ Primary Examiner, Art Unit 1658