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 .
Priority
This application was filed on and is a U.S. national Stage application under 35 U.S.C. 371 of International Patent Application No. PCT/KR2019/018316 filed 12/23/2019, which claims the benefit of the priority of Korean Patent Application No. 10-2018-0167698 filed 12/21/2018.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Claim Status
Claims 1-6, 8-9, 23-25, 30, 32, 34-37, 41-43, and 61-63 are pending. Claims 1, 23-24, 30, 32, 34-35, 37 are amended. Claims 63 is new. Claims 1-6, 8-9, 23-25, 30, 32, 34-37, 41-43, and 61-63 are being examined on the merits in this office action.
Claim Rejections Withdrawn
The rejection of claims 24 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, is withdrawn in view of the claim amendments.
The rejection of claim 37 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, is withdrawn in view of the claim amendments.
The rejection of claims 30, 32, 34, and 35 under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, is withdrawn in view of the claim amendments.
Claim Objections - Withdrawn
The objection claims 1, 23, 30, 34, and 37 is withdrawn in view of the amendments.
Claim Rejections - 35 USC § 103 – Maintained and updated
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 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.
Claims 1-6, 8-9, 23-25, 30, 32, 35-37, 41-43, and 61-63 are rejected under 35 U.S.C. 103 as being unpatentable over DiMarchi et al. (WO2016/049190A1 – hereinafter “DiMarchi”, cited and enclosed in previous office action) in view of Oh et al. (WO2017116204A1 – hereinafter “Oh”, cited and enclosed in previous office action) and Jin et al. (KR20180090760A – hereinafter “Jin”, cited and enclosed in previous office action).
The teaching of the Oh et al. (WO2017116204A1) publication are based on the English language translation of the WO2017116204A1 publication obtained by Google patent and the citations are based on the English language translation.
This rejection has been updated to include new claim 63.
Claim Interpretation
Examiner notes that the instant claims require insulin. The instant specification does not define or distinguish insulin from the plain and ordinary definition of the term insulin as being native insulin. Examiner further notes that the teachings of DiMarchi disclose an insulin agonist peptide and DiMarchi defines an insulin agonist peptide to include “native insulin or any known insulin analog that has activity at the insulin receptor including for example any insulin peptide disclosed in published international applications W096/34882, WO 2010/080607, WO 2010/080609, WO 2011/159882, WO/2011/159895 and US Patent No. 6,630,348, the disclosures of which are incorporated herein by reference.” Further, DiMarchi teaches the instant insulin sequence as recited in claim 28. Examiner therefore concludes that the insulin agonist peptide of DiMarchi reads on the instant insulin.
Dimarchi teaches an incretin-insulin conjugate comprising an incretin peptide; and an insulin agonist peptide (claim 1), wherein the insulin peptide is a two-chain insulin analog comprising a B chain and an A chain, wherein said B chain is linked to said A chain through disulfide linkages (claim 9), wherein the incretin peptide of SEQ ID NO: 1931 (claim 21, 23). DiMarchi further teaches pharmaceutical compositions that comprises the conjugates and a pharmaceutically acceptable carrier (Page 13, line 14-16). DiMarchi teaches insulin peptide comprises an A chain sequence of GIVEQCCTSICSLYQLENYCN-R13 (SEQ ID NO: 1) and a B chain sequence selected from the group consisting of FVNQHLCGSHLVEALYLVCGERGFFYTPKT (SEQ ID NO: 2), FVNQHLCGSHLVEALYLVCGERGFFYTKPT (SEQ ID NO: 9), FVNQHLCGSHLVEALYLVCGERGFFYTDKT (SEQ ID NO: 5), and FVKQHLCGSHLVEALYLVCGERGFFYTEKT (SEQ ID NO: 6) (Claim 23) which reads on the instant formulas. DiMarchi teaches that the composition for use to decrease appetite and reduce blood glucose (Page 3, line 10-11).
DiMarchi does not teach the instant incretin peptide of SEQ ID NO: 42-43, or 96-97.
However, the sequence recited in independent claim 1 are known in the art as taught by Oh et al.
Oh teaches a peptide having activity against glucagon receptor, Glucagon-like peptide-1 receptor, and Glucose-dependent insuliontropic polypeptide receptor, that the peptide is derived from a native GLP-1, native GIP, or native exendin-4 amino acid sequence, that the peptide has the Formula 1. SEQ ID NO: 103 (claims 1, 3-4). Oh teaches that the pharmaceutical composition for preventing or treating metabolic syndrome, comprising the peptide of any one of claims 1 to 13 and specifically for treating disorders of glucose tolerance, hypercholesterolemia, dyslipidemia, obesity, diabetes (claims 20-21). Oh teaches SEQ ID NO: 43 (Example 1 on page 22). Examiner notes that this sequence is 100% identical to the instant SEQ ID NO: 42.
Further, Jin teaches a conjugate that comprises a physiologically active substance, a linker and a substance that can increase the half-life (claim 1), that the physiologically active substance includes GLP-1 receptor agonists or insulin (claims 6-7), that the insulin analogue comprises the sequence of SEQ ID NO: 3 which is identical to the instant SEQ ID NO: 119. Thus, Jin teaches a similar composition that is taught by DiMarchi.
Jin teaches that the insulin analogue the A chain of SEQ ID NO: 3 represented by the following general formula 1 and the B chain of SEQ ID NO: 4 represented by the following general formula 4 and that [Formula 1] is
Xaa1-Xaa2-Val-Glu-Gln-Cys-Cys-Thr-Ser-Ile-Cys-Ser- Leu-Xaa14-Gln- Leu- Glu- Asn- Xaa19-Cys- Asn (SEQ ID NO: 3), wherein, Xaa1 is glycine or alanine, Xaa2 is isoleucine or alanine, Xaa14 is tyrosine, glutamic acid or asparagine, Xaa19 is tyrosine or alanine [0082-0083]; and that formula 4 is Phe-Val-Asn-Gln- His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu- Xaa16 -Leu-Val-Cys-Gly-Glu-Arg-Gly-Phe- Xaa25 - Tyr- Xaa27 - Xaa28- Lys-Thr (SEQ ID NO: 6), wherein, Xaa16 is a tyrosine, Xaa25 is phenylalanine, Xaa27 is threonine, Xaa28 is proline [0122-0128].
Jin further teaches the insulin analogue is selected from the group consisting of amino acid 1, amino acid 2, amino acid 3, amino acid 5, amino acid 8, amino acid 10, amino acid 12, amino acid 16, amino acid 23, The amino acid of SEQ ID NO: 24, amino acid 25, amino acid 26, amino acid 27, amino acid 28, amino acid 29, amino acid 30, amino acid 1 of the A chain, amino acid 2, amino acid 5, amino acid 8, amino acid 10 wherein one or more amino acids selected from the group consisting of amino acids 12, 14, 16, 17, 18, 19, and 21 are substituted or deleted with other amino acids (claim 9).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the composition of DiMarchi and use the peptide having GLP-1 activity of Oh and the insulin analogues taught by Jin since Oh teaches that the peptide displayed an increase in half-life compared to any one of native GLP-1, native glucagon, and native GIP (claim 17) and Jin teaches that insulin analogue has reduced insulin receptor binding ability as compared to native type insulin [0067]. One of ordinary skill in the art would be motivated and would have had a reasonable expectation of success in using the peptide of Oh and Jin since both references teach a composition comprising insulin and a peptide having activity on the GLP-1 receptor; activation of glucagon receptor and activation of GIP receptors. The cited references render obvious claim 1.
Regarding claims 2-3, DiMarchi teaches that the insulin analog is conjugated to an incretin peptide of SEQ ID NO: 1931 (claims 1, 21, 23) and that the incretin peptide improves duration of action or half-life in circulation (page 13, line 3-4; page 23, line 25-26; page 24, line 1-2; page 76, line 25-26;page 108, line 9-10. DiMarchi further teaches that the insulin analog had a better half-life (Page 175, line 10-11; page 176, line 1-3; Table 11).
Regarding claim 4, Dimarchi teaches an incretin-insulin conjugate comprising an incretin peptide; and an insulin agonist peptide (claim 1), wherein the insulin peptide is a two-chain insulin analog comprising a B chain and an A chain, wherein said B chain is linked to said A chain through disulfide linkages (claim 9). DiMarchi teaches that the insulin analog is conjugated to an incretin peptide of SEQ ID NO: 1931 (claims 1, 21, 23) and that the incretin peptide improves duration of action or half-life in circulation (page 13, line 3-4; page 23, line 25-26; page 24, line 1-2; page 76, line 25-26; page 108, line 9-10. DiMarchi further teaches that the insulin analog had a better half-life (Page 175, line 10-11; page 176, line 1-3; Table 11).
Regarding claim 5, DiMarchi teaches the composition administered to insulin dependent patients while increasing weight loss or preventing weight gain is provided (Page 13, line 30-33).
Regarding claim 6, DiMarchi teaches administering the composition comprising the conjugate to a patient for the treatment of diabetes (claims 43-44). DiMarchi further teaches that the incretin-insulin conjugates described herein can be used to treat hyperglycemia, or treat other metabolic diseases that result from high blood glucose levels.
Regarding claims 8-9, Dimarchi teaches that the pharmaceutical composition comprises a 1mg/ml concentration of the incretin-insulin conjugate [0375]. Examiner notes DiMarchi thus shows one incretin conjugated to one insulin, and since incretin is GLP-1, the teaching reads on a 1:1 ratio thus anticipating claims 8-9.
Regarding claim 23, Oh teaches specifically the peptide of SEQ ID NO: 64 YXQGTFTSDYSKYLDEKRAKEFVQWLLDHHPSSGQPPPSC (SEQ ID NO: 42), wherein X is AIB (Example 1). Examiner notes that this sequence is 100% identical to the instant SEQ ID NO: 42. It would have been obvious to modify the sequence of DiMarchi with the sequence of Oh since both references teach similar analogs in a composition with insulin.
Regarding claim 24, Oh teaches that the amino acids 16 and 20 from the N-terminus in the general formula form a ring with each other (Page 11).
Regarding claim 25, Oh teaches that the peptide C-terminus is amidated (claim 18). It would have been obvious to modify the sequence of DiMarchi and amidate it at the C-terminus as taught by Oh since both references teach similar analogs in a composition with insulin.
Regarding claim 30, the cited references render obvious the instant composition. Further, Jin teaches the sequence of Formula 4 [0122-0123] in combination with the Fc region [0491-0495] which reads on SEQ ID NO: 124 and 142. DiMarchi teaches that the composition for use to decrease appetite and reduce blood glucose (Page 3, line 10-11). It would be obvious to modify the insulin analog of DiMarchi to include an Fc region thus arriving to the instant sequence as taught by Jin.
Regarding claim 32, Jin teaches the sequence of Formula 4 [0122-0123] in combination with the Fc region [0491-0495] which reads on SEQ ID NO: 124 and 142. DiMarchi teaches that the composition for use to decrease appetite and reduce blood glucose (Page 3, line 10-11). It would be obvious to modify the insulin analog of DiMarchi to include an Fc region thus arriving to the instant sequence as taught by Jin.
Regarding claim 35, Jin teaches insulin analogue is characterized by comprising the A chain of SEQ ID NO: 3 represented by the following general formula 1 and the B chain of SEQ ID NO: 4 represented by the following general formula 2 [0080], which are identical to the instant sequences. DiMarchi teaches that the composition for use to decrease appetite and reduce blood glucose (Page 3, line 10-11). It would have been obvious to modify the insulin of DiMarchi with the amino acid substitutions taught by Jin, since Jin teaches a similar composition to DiMarchi that comprises insulin and GLP-1 thus arriving to the instant sequence of claim 35.
Regarding claim 36, Jin teaches that the A chain and the B chain sequences may be mutually connected by a disulfide bond [0342, 0369]. It would have been obvious to modify the insulin of DiMarchi and connect by a disulfide bond as taught by Jin.
Regarding claims 37, 40-42, and 63, Jin teaches a conjugate that comprises a physiologically active substance (X), a linker (L) and a substance that can increase the half-life (F) (claim 1), that the physiologically active substance includes GLP-1 receptor agonists or insulin (claims 1, 6-7), and that F is an immunoglobulin Fc region or an IgG Fc region (claims 13-15) can be modified by glycosylation [0497]. It would have been obvious to modify the conjugate of DiMarchi with the teachings of Jin since Jin teaches that the conjugate displayed advantages such as increased half-life (Abstract).
Regarding claim 43, Jin teaches that the immunoglobulin Fc region of the present invention comprises 1) CH1 domain, CH2 domain, CH3 domain and CH4 domain, 2) CH1 domain and CH2 domain, 3) CH1 domain and CH3 domain, 4) CH2 domain and CH3 domain, 5 ) Combination of an immunoglobulin hinge region (or a portion of a hinge region) with one or more of the CH1 domain, CH2 domain, CH3 domain and CH4 domain (e.g., a CH2 domain and a CH3 domain and a hinge region or a portion thereof) Combinations, and combinations of the above.) 6) The heavy chain constant region may be a dimer of an angular domain and a light chain constant region [0493]. It would have been obvious to modify the conjugate of DiMarchi with the teachings of Jin since Jin teaches that the conjugate displayed advantages such as increased half-life (Abstract).
Regarding claim 61, Jin teaches that L is a linker, a polyethylene glycol [0182].
Regarding claim 62, Jin teaches the conjugate according to the present invention is useful for the treatment of diabetes, and by administering the pharmaceutical composition containing the conjugate [0546].
Claim 34 is rejected under 35 U.S.C. 103 as being unpatentable over DiMarchi et al. (WO2016/049190A1 – hereinafter “DiMarchi”, cited and enclosed in previous office action ) in view of Oh et al. (WO2017116204A1 – hereinafter “Oh”, cited and enclosed in previous office action) and Jin et al. (KR20180090760A – hereinafter “Jin”, cited and enclosed in previous office action), as applied to claim 1 above, and further in view of Choi et al. (US20180291077A1 – hereinafter “Choi”, cited and enclosed in previous office action).
The teachings of DiMarchi, Oh, and Jin are disclosed above and incorporated herein by reference. Even though both DiMarchi and Jin teach proinsulin, DiMarchi and Jin do not teach the proinsulin sequence as recited in the instant claim 34.
Choi teaches insulin analogs and methods of preparing (Abstract) and that the analogs have the sequence including the sequence of SEQ ID NO: 46 (See Table 1, Analog 21) which is 100% identical to the instant SEQ ID NO: 168.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the teachings of DiMarchi and Jin and use the insulin analog of Choi since both DiMarchi and Jin teach composition comprising insulin and GLP-1 and further teach analogs including proinsulin. One of ordinary skill in the art would be motivated and would have had a reasonable expectation of success modifying the insulin analogue as taught by DiMarchi and Jin since Choi teaches that the insulin analogs may possess in vivo blood glucose level-controlling capability equivalent or corresponding to that of native insulin [0067]. The disclosures render obvious claim 34.
Response to Arguments
Applicant's arguments filed 12/12/2025 have been fully considered but they are not persuasive.
Applicant argues that the working examples demonstrate that when a long- acting conjugate of insulin is co-administered with a long-acting conjugate of a triple agonist having activity to glucagon, GLP-1, and GIP receptors, blood glucose control is superior and insulin-induced weight gain is effectively improved compared to each administered alone.
Applicant argues that DiMarchi is limited to the GLP-1 family, and thus simultaneous action on glucagon and GIP receptors (glucagon GLP-1 GIP triple activity) is not considered at all and that the inventive concept of a co-administration composition of "insulin + glucagon GLP-1 GIP triple agonist" as in the present claims cannot be derived from DiMarchi. Applicant argues that Oh does not teach co-administration.
The arguments presented above have been fully considered but are unpersuasive. Examiner notes that the instant claims are drawn to a composition comprising insulin and an isolated peptide having activity to glucagon, glucagon-like peptide-1 (GLP-1), and glucose-dependent insulinotropic polypeptide (GIP) receptors. The instant claims do not limit the composition to just co-administration. The claims only require that the composition comprise insulin and the isolated peptide. Further, the triple agonist is known in the art as taught by Oh. One of ordinary skill in the art would be motivated to use or modify DiMarchi and use the triple agonist so to target all of GLP-1, GIP, and glucagon receptors simultaneously.
Regarding the argument of superior results, Examiner notes that DiMarchi teaches that the composition was effective in regulating blood glucose levels while increasing weight loss or preventing weight gain is provided. Specifically, Fig. 17 and 34 of DiMarchi showed improved blood glucose levels and weight similar to the data indicated in the instant invention. The arguments are unpersuasive.
Double Patenting - Maintained
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The 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, 5, 23, 25, 30, 32, 35-37, 40-43, and 61-62 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 100, 125-129, 131-134, and 136, of copending Application No. 17/282,661. Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of the copending application recite a method that comprises administering a composition that comprises a substance with activity to a glucagon receptor or a conjugate thereof which is co-administered with a compound or substance with therapeutic activity against the metabolic syndrome (claim 100) that substance with activity to a glucagon receptor is a peptide comprising an amino acid sequence of General Formula 1 (claims 125-126-129), and that compound with therapeutic activity comprises insulin (claim 138).
The instant claims recite a composition comprising (i) insulin; and (ii) an isolated peptide having activity to glucagon, glucagon-like peptide-1 (GLP-1), and glucose-dependent insulinotropic polypeptide (GIP) receptors, wherein the peptide comprises an amino acid sequence represented by Formula 1 (claim 1), wherein the insulin is native insulin, or an insulin analog comprising an A-chain of SEQ ID NO: 119 of the following Formula 4; and a B-chain of SEQ ID NO: 120 of the following Formula 5, and wherein the isolated peptide having activity to glucagon, GLP-1, and GIP receptors comprises an amino acid sequence selected from SEQ ID NOS: 42, 43, 96, and 97.
The difference between the claims of the copending application and the instant claims is that the claims of the copending application do not recite the insulin sequence.
However, a composition comprising insulin and incretin is known in the art as taught by Jin et al. Jin teaches a conjugate that comprises a physiologically active substance, a linker and a substance that can increase the half-life (claim 1), that the physiologically active substance includes GLP-1 receptor agonists or insulin (claims 6-7), that the insulin analogue comprises the sequence of SEQ ID NO: 3 which is identical to the instant SEQ ID NO: 119. Jin teaches that the insulin analogue the A chain of SEQ ID NO: 3 represented by the following general formula 1 and the B chain of SEQ ID NO: 4 represented by the following general formula 4 and that [Formula 1] is
Xaa1-Xaa2-Val-Glu-Gln-Cys-Cys-Thr-Ser-Ile-Cys-Ser- Leu-Xaa14-Gln- Leu- Glu- Asn- Xaa19-Cys- Asn (SEQ ID NO: 3), wherein, Xaa1 is glycine or alanine, Xaa2 is isoleucine or alanine, Xaa14 is tyrosine, glutamic acid or asparagine, Xaa19 is tyrosine or alanine [0082-0083]; and that formula 4 is Phe-Val-Asn-Gln- His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu- Xaa16 -Leu-Val-Cys-Gly-Glu-Arg-Gly-Phe- Xaa25 - Tyr- Xaa27 - Xaa28- Lys-Thr (SEQ ID NO: 6), wherein, Xaa16 is a tyrosine, Xaa25 is phenylalanine, Xaa27 is threonine, Xaa28 is proline [0122-0128]. Jin further teaches the insulin analogue is selected from the group consisting of amino acid 1, amino acid 2, amino acid 3, amino acid 5, amino acid 8, amino acid 10, amino acid 12, amino acid 16, amino acid 23, The amino acid of SEQ ID NO: 24, amino acid 25, amino acid 26, amino acid 27, amino acid 28, amino acid 29, amino acid 30, amino acid 1 of the A chain, amino acid 2, amino acid 5, amino acid 8, amino acid 10 wherein one or more amino acids selected from the group consisting of amino acids 12, 14, 16, 17, 18, 19, and 21 are substituted or deleted with other amino acids (claim 9).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the claims of the copending application and use the insulin analogues taught by Jin since Jin teaches that insulin analogue has reduced insulin receptor binding ability as compared to native type insulin [0067]. One of ordinary skill in the art would be motivated and would have had a reasonable expectation of success in using the insulin sequence of Jin since the reference teaches a composition comprising insulin and a peptide having activity on the GLP-1 receptor; activation of glucagon receptor and activation of GIP receptors.
Regarding claims 5, and 62, the claims of the copending application recite a subject in need thereof a pharmaceutical composition comprising a substance with activity to a glucagon receptor or a conjugate thereof, which is likely to be co-administered with a compound or substance with therapeutic activity against the metabolic syndrome (claim 100)
Regarding claims 23 and 25, the claims of the copending application recite wherein that substance with activity to a glucagon receptor is a peptide comprising an amino acid sequence of General Formula 1 (claim 125-126-129),
Regarding claim 30, Jin teaches the sequence of Formula 4 [0122-0123] in combination with the Fc region [0491-0495] which reads on SEQ ID NO: 124 and 142. It would be obvious to modify the claims of the copending application insulin analog to include an Fc region thus arriving to the instant sequence as taught by Jin.
Regarding claim 32, Jin teaches the sequence of Formula 4 [0122-0123] in combination with the Fc region [0491-0495] which reads on SEQ ID NO: 124 and 142. It would be obvious to modify the claims of the copending application insulin analog to include an Fc region thus arriving to the instant sequence as taught by Jin.
Regarding claim 35, Jin teaches insulin analogue is characterized by comprising the A chain of SEQ ID NO: 3 represented by the following general formula 1 and the B chain of SEQ ID NO: 4 represented by the following general formula 2 [0080], which are identical to the instant sequences. ]. It would have been obvious to modify the claims of the copending application insulin analog with the amino acid substitutions taught by Jin, thus arriving to the instant sequence of claim 35.
Regarding claim 36, Jin teaches that the A chain and the B chain sequences may be mutually connected by a disulfide bond [0342, 0369]. It would have been obvious to modify the insulin of the claims of the copending application and connect by a disulfide bond as taught by Jin.
Regarding claims 37, 40-43, 61, the claims of the copending application recite wherein the compound with therapeutic activity comprises insulin (claim 138), which is linked to the peptide by a biocompatible material such as a polymer like PEG (claims 130-135), wherein the the immunoglobulin Fc region is aglycosylated, wherein the immunoglobulin Fc region comprises one selected from the group consisting of: (a) CH1 domain, CH2 domain, CH3 domain, and CH4 domain; (b) CH1 domain and CH2 domain; (c) CH1 domain and CH3 domain; (d) CH2 domain and CH3 domain; (e) a combination of one or more domains selected from the CH1 domain, CH2 domain, CH3 domain, and CH4 domain and an immunoglobulin hinge region or a part of the hinge region; and (f) a dimer of each domain of the heavy chain constant region and the light chain constant region; wherein the immunoglobulin Fc region is an IgG4 Fc region (claim 136).Examiner herein incorporates all the limitations of claims 121-126, 128-129, 131-134, 136, 139 because these claims recite similar limitations as the instant claims 2-3, 11-12,15, 17, 20-23, and 25.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicant's argument has been fully considered but is not found persuasive because only compliance with objections or requirements as to form not necessary for further consideration of the claims may be held in abeyance until allowable subject matter is indicated. MPEP §804. Therefore, the nonstatutory double patenting rejections are maintained.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any 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 Mercy H. Sabila whose telephone number is (571)272-2562. The examiner can normally be reached Monday - Friday 5:00 am - 3:00 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko G. Garyu can be reached at (571)270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/MERCY H SABILA/Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654