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 . 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.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 7 Nov, 2025 has been entered.
Election/Restrictions
Applicants elected condensing SEQ IDs 7, 11, and 20 without traverse in the reply filed on 11 Nov, 2024.
Claims Status
Claims 2, 4, 39, and 40 are pending.
Claims 2 and 40 have been amended.
Maintained/Modified Rejections
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) 2, 4, 39, and 40 are rejected under 35 U.S.C. 103 as being unpatentable over Alsina-Fernandez et al (WO 2019125938, cited by applicants) in view of Bray (Nat. Rev. Drug Discov. (2003) 2 p587-593, cited by applicants) and Leng et al (CN 103864918). Note that Leng et al is in Chinese. A machine translation is relied upon, and references to locations in the document in this rejection refer to the machine translation.
Alsina-Fernandez et al discuss incretin analogs with activity at each of the GIP, GLP-1, and glucagon receptors, which have an extended duration of action at each receptor (abstract). They are useful for enhancing glucose control, weight loss, lipid benefits, and other disorders (p2, 4th paragraph). Among the compounds synthesized is SEQ ID 17 (p21, 2nd paragraph), identical with SEQ ID 6 of the examined application. It has appropriate binding at all three receptors (table 2, p26, bottom of page, continues to p27, and p27, 1st paragraph), is functional at all three receptors (table 3, p28, bottom of page, continues to p29 and p29, 1st paragraph), including when there is a blocking reagent (table 4, p29, bottom of page, continues to p30, and p30, 1st paragraph), has extended pharmacokinetic profile in mice (table 5, p30, bottom of page, continues to p31), gives a dose dependent response on insulin secretion (table 6, p32, top of page, p32, 1st paragraph), causes weight loss in a mouse model of obesity in a dose dependent manner (table 7, p33, bottom of page, and p34, 1st paragraph), and improves blood chemistry (table 8, p34, 2nd paragraph, p34, 3d paragraph). Synthesis was standard solid phase synthesis, using standard side chain protecting groups (p14, 2nd paragraph).
The difference between this reference and the examined claims is that this reference uses a different synthesis protocol.
Bray discusses large scale manufacture of peptides (title). Synthesis of fragments is conducted on solid phase using acid sensitive resin to make protected fragments, which can then be coupled either on resin (solid phase) or in solution (p589, 1st column, 2nd paragraph). Fragment selection is crucial; selection is based on solubility, ease of synthesis, purity, yield, and the carboxyl terminus are considered, but the ideal fragments can only be determined by trial and error (p590, 3d column, 2nd paragraph). In the example of enfuviratide, the side chain protection is boc (for Lys residues), tBtu for Tyr, Thr, Ser, Glu, and Asp residues, and trt for Gln residues (fig 3, p591, right of page). Note that, because of the large number of reactions in peptide synthesis, a small difference in yield or purity at each step can make large differences in the final product (p592, 2nd column, 3d paragraph). This reference discusses scale up of peptide synthesis using fragment condensation methods.
Leng et al discusses the synthesis of liraglutide (title), a GLP-1 analog (paragraph 23), an incretin. Note that K20 has a fatty acid modification with a Glu linker (paragraph 27). The synthesis method was to synthesize the fragment containing K20 with an MTT protecting group (paragraph 66), followed by removing the MTT protecting group and adding the protected side chain modification (paragraph 77). This was then coupled with the remaining fragments to generate the finished polypeptide (paragraph 82). This reference discusses fragment based synthesis of a polypeptide with a side chain modification.
Therefore, it would be obvious to try the various combinations of fragments to find the best in terms of ease of synthesis, purity, and yield, as discussed by Bray. As Bray states that this is to be determined by trial and error (i.e. trying the possibilities to find the best), an artisan in this field would attempt this process with a reasonable expectation of success.
Furthermore, it would be obvious to generate the protected fragment containing K17 with the side chain modification of that amino acid on the fragment, as Leng et al used a similar protocol for synthesis of their incretin. As the side chain is similar in both cases (Glu attached to a fatty acid), an artisan in this field would attempt this synthesis with a reasonable expectation of success.
Alsina-Fernandez et al discusses a polypeptide identical with SEQ ID 6 (as interpreted). Bray discusses optimizing the synthesis using fragment condensation, and mention solid/liquid hybrid synthesis. Bray also mentions the same protecting group strategy as applicants, and Leng et al discusses adding the side chain modification before condensation. As every possible combination of fragments is attempted, the condensation of SEQ IDs 7, 11, and 20 will be attempted. Thus, the combination of references renders obvious claims 2, 4, 39, and 40.
response to applicant’s arguments
Applicants argue that fragment 20 is longer than would be selected for fragment condensation, that the fatty acid would be expected to negatively affect solubility excessively, that the steric hinderance of the Aib residue at the C-terminus of fragment 20 would be predicted to be disadvantageous, claim the unexpected result of rapid coupling, argue that the cited prior art would not lead to the claimed method, and that there is no motivation and no reasonable expectation of success. This is supported by a declaration by Prof. Michael Kopach, applicant.
Applicant's arguments filed 7 Nov, 2025 have been fully considered but they are not persuasive.
Applicants argue that fragments as long as SEQ ID 20 would not be selected for fragment condensation. This argument makes no logical sense. For synthesis by fragment coupling, eventually, there will be a final coupling step between two fragments to generate a final product. If the final sequence is long, at least one of the fragments will be long, even if it was generated by coupling smaller fragments.
Applicants argue that the fatty acid modification of the lysine would be expected to make the solubility too poor to use. However, Leng et al used a similar fatty acid modification, and was successfully coupled. It is not clear from the record why this would be considered by a person of skill in the art to be fatal to the synthesis, given this example. Note that the Fisher Scientific catalog page for C20 acid (downloaded 23 Feb, 2026) lists the compound as soluble in chloroform and DMF; so would reasonably be expected to not cause solubility problems during synthesis.
Applicants argue that the steric hinderance of the Aib on the C-terminus of SEQ ID 20 would be disadvantageous. It is not clear how using a fragment with Aib somewhere other than the C-terminus would be helpful; the same issue would occur when making the fragment. Applicants argue that the rest of SEQ ID 20 would not be there, so there would be less steric hinderance, but that argument assumes that the protecting group has minimal steric hinderance. It is not clear that a relatively large Fmoc group (used by Jad et al in different sets of arguments), which is right at the amine of Aib will be much less sterically hindered than SEQ ID 20. While SEQ ID 20 is larger than an Fmoc group, the bulk is further away from the reaction center. Moving a potential problem to a different synthesis step does not clearly improve the synthesis. Applicants argue that Jad et al does not support the argument that it is possible to couple Aib residues, because it is coupling a single residue, is using protocols for steric hinderance, and some of the reactions show significant amounts of uncoupled material. The fact that Jad et al is using Fmoc-Aib rather than Aib on the C-terminus of a fragment, as noted above, would not lead a person to categorically assume that there would be too much steric hinderance, as noted above. Applicant’s argument that Jad et al uses a protocol for sterically hindered peptides is also not persuasive. It is not clear that this is due to steric hinderance, is just a default protocol for the lab, or was just the resin that was closest to hand. Nor is it clear how, even if this was used to improve yield of a sterically hindered peptide, it would overcome the rejection. It is not debated that Aib is a sterically hindered amino acid, and that the steric hinderance can play a role in synthesis. Applicants argue that the sequence of Jad et al did not synthesize well, with large amounts of a des-Aib sequence. However, this sequence was selected as a very difficult synthesis sequence, as a difficult test for different solvents in synthesis (p6812, 1st column, 2nd paragraph). The fact that the authors can get yields similar to those of applicants with essentially minor optimization would tend to promote the idea that it is possible to couple Aib residues. Applicants point to couplings with Aib that were problematic, but there are a few issues with that argument. First, it is not clear that a person of skill in the art would have access to those documents as of applicant’s priority date. Second, the fact that a different sequence was difficult does not mean that a person of skill in the art would assume applicant’s sequence would be difficult; as noted in both the prior art and applicant’s declaration, this is not something that can be predicted a priori.
It should be noted that applicants are ignoring portions of the prior art that would encourage Aib at the C-terminus, that is, a residue not prone to epimerization (Bray et al, p590, 3d column, 2nd paragraph, Nyfler, p307, 2nd paragraph). Note that Nyfler (cited by applicants) explicitly suggests Pro residues at the C-terminus to reduce racemization (p307, 2nd paragraph). This residue has comparable steric hinderance to Aib.
Finally, applicants argue that it is unexpected that the reaction proceeds rapidly and effectively. It is not clear why this would be surprising. As noted previously, coupling with Aib has been successful in the prior art, even with sequences that are considered difficult.
Applicants argue that the cited references would not lead to the claimed sequences. The rejection uses Bray’s statement of experimentation to find the best fragments to support an obvious to try rationale. Applicants argue that Bray does not discuss the issues that applicants bring up, so it would not lead to applicant’s claimed fragments. However, if every fragment is tested for the effects discussed by Bray (solubility, ease of synthesis, purity, yield, p590, 3d column, 2nd paragraph), it will necessarily encompass applicant’s claimed sequences.
Finally, applicants argue that there is no motivation and no reasonable expectation of success. There are two pieces of this argument; the first is that it is not possible to a priori predict the best fragments for coupling, and that this would require too many additional steps. It is not clear how these arguments overcome the rejection; if every possible fragment is tested, clearly, the best fragments must be tested. Applicants argue that many time and resource intensive steps would remain, but that is a different question than the best fragment. Applicants point to a court decision that states that discusses an improper obvious to try rejection, but applicants have not made an argument that this is such a rejection.
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.
first rejection
Claims 2, 4, 39, and 40 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of U.S. Patent No. 12,496,329 n view of Bray (Nat. Rev. Drug Discov. (2003) 2 p587-593, cited by applicants) and Leng et al (CN 103864918). Note that Leng et al is in Chinese. A machine translation is relied upon, and references to locations in the document in this rejection refer to the machine translation.
Competing claim 85 describes a method of weight management, comprising administering a polypeptide of SEQ ID 1, identical with SEQ ID 6 of the examined claims.
The difference between the competing claims and the examined claims is that the competing claims do not discuss synthesis of this sequence.
Bray discusses large scale manufacture of peptides (title). Synthesis of fragments is conducted on solid phase using acid sensitive resin to make protected fragments, which can then be coupled either on resin (solid phase) or in solution (p589, 1st column, 2nd paragraph). Fragment selection is crucial; selection is based on solubility, ease of synthesis, purity, yield, and the carboxyl terminus are considered, but the ideal fragments can only be determined by trial and error (p590, 3d column, 2nd paragraph). In the example of enfuviratide, the side chain protection is boc (for Lys residues), tBtu for Tyr, Thr, Ser, Glu, and Asp residues, and trt for Gln residues (fig 3, p591, right of page). Note that, because of the large number of reactions in peptide synthesis, a small difference in yield or purity at each step can make large differences in the final product (p592, 2nd column, 3d paragraph). This reference discusses scale up of peptide synthesis using fragment condensation methods.
Leng et al discusses the synthesis of liraglutide (title), a GLP-1 analog (paragraph 23). In other words, and incretin. Note that K20 has a fatty acid modification with a Glu linker (paragraph 27). The synthesis method was to synthesize the fragment containing K20 with an MTT protecting group (paragraph 66), followed by removing the MTT protecting group and adding the protected side chain modification (paragraph 77). This was then coupled with the remaining fragments to generate the finished polypeptide (paragraph 82). This reference discusses fragment based synthesis of a polypeptide with a side chain modification.
Therefore, it would be obvious to try the various combinations of fragments to find the best in terms of ease of synthesis, purity, and yield, as discussed by Bray. As Bray states that this is to be determined by trial and error (i.e. trying the possibilities to find the best), an artisan in this field would attempt this process with a reasonable expectation of success.
Furthermore, it would be obvious to generate the protected fragment containing K17 with the side chain modification of that amino acid on the fragment, as Leng et al used a similar protocol for synthesis of their incretin. As the side chain is similar in both cases (Glu attached to a fatty acid), an artisan in this field would attempt this synthesis with a reasonable expectation of success.
This is a provisional nonstatutory double patenting rejection.
response to applicant’s arguments
Applicants have referred to the arguments made with respect to the rejection under 35 USC 103, above, which were discussed there.
second rejection
Claims 2, 4, 39, and 40 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/552,013 (US 20240173250) in view of Bray (Nat. Rev. Drug Discov. (2003) 2 p587-593, cited by applicants) and Leng et al (CN 103864918). Note that Leng et al is in Chinese. A machine translation is relied upon, and references to locations in the document in this rejection refer to the machine translation.
Competing claim 1 describes a formulation comprising a polypeptide of SEQ ID 1, identical with SEQ ID 6 of the examined claims.
The difference between the competing claims and the examined claims is that the competing claims do not discuss synthesis of this sequence.
Bray discusses large scale manufacture of peptides (title). Synthesis of fragments is conducted on solid phase using acid sensitive resin to make protected fragments, which can then be coupled either on resin (solid phase) or in solution (p589, 1st column, 2nd paragraph). Fragment selection is crucial; selection is based on solubility, ease of synthesis, purity, yield, and the carboxyl terminus are considered, but the ideal fragments can only be determined by trial and error (p590, 3d column, 2nd paragraph). In the example of enfuviratide, the side chain protection is boc (for Lys residues), tBtu for Tyr, Thr, Ser, Glu, and Asp residues, and trt for Gln residues (fig 3, p591, right of page). Note that, because of the large number of reactions in peptide synthesis, a small difference in yield or purity at each step can make large differences in the final product (p592, 2nd column, 3d paragraph). This reference discusses scale up of peptide synthesis using fragment condensation methods.
Leng et al discusses the synthesis of liraglutide (title), a GLP-1 analog (paragraph 23). In other words, and incretin. Note that K20 has a fatty acid modification with a Glu linker (paragraph 27). The synthesis method was to synthesize the fragment containing K20 with an MTT protecting group (paragraph 66), followed by removing the MTT protecting group and adding the protected side chain modification (paragraph 77). This was then coupled with the remaining fragments to generate the finished polypeptide (paragraph 82). This reference discusses fragment based synthesis of a polypeptide with a side chain modification.
Therefore, it would be obvious to try the various combinations of fragments to find the best in terms of ease of synthesis, purity, and yield, as discussed by Bray. As Bray states that this is to be determined by trial and error (i.e. trying the possibilities to find the best), an artisan in this field would attempt this process with a reasonable expectation of success.
Furthermore, it would be obvious to generate the protected fragment containing K17 with the side chain modification of that amino acid on the fragment, as Leng et al used a similar protocol for synthesis of their incretin. As the side chain is similar in both cases (Glu attached to a fatty acid), an artisan in this field would attempt this synthesis with a reasonable expectation of success.
This is a provisional nonstatutory double patenting rejection.
response to applicant’s arguments
Applicants have referred to the arguments made with respect to the rejection under 35 USC 103, above, which were discussed there.
third rejection
Claims 2, 4, 39, and 40 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 8, and 18 of U.S. Patent No. 11,542,313 in view of Bray (Nat. Rev. Drug Discov. (2003) 2 p587-593, cited by applicants) and Leng et al (CN 103864918). Note that Leng et al is in Chinese. A machine translation is relied upon, and references to locations in the document in this rejection refer to the machine translation.
Competing claim 1 describes a genus of peptides with competing claim 8 describing a narrower genus, and claim 18 describing a polypeptide identical with SEQ ID 6 of the examined claims.
The difference between the competing claims and the examined claims is that the competing claims do not discuss synthesis of this sequence.
Bray discusses large scale manufacture of peptides (title). Synthesis of fragments is conducted on solid phase using acid sensitive resin to make protected fragments, which can then be coupled either on resin (solid phase) or in solution (p589, 1st column, 2nd paragraph). Fragment selection is crucial; selection is based on solubility, ease of synthesis, purity, yield, and the carboxyl terminus are considered, but the ideal fragments can only be determined by trial and error (p590, 3d column, 2nd paragraph). In the example of enfuviratide, the side chain protection is boc (for Lys residues), tBtu for Tyr, Thr, Ser, Glu, and Asp residues, and trt for Gln residues (fig 3, p591, right of page). Note that, because of the large number of reactions in peptide synthesis, a small difference in yield or purity at each step can make large differences in the final product (p592, 2nd column, 3d paragraph). This reference discusses scale up of peptide synthesis using fragment condensation methods.
Leng et al discusses the synthesis of liraglutide (title), a GLP-1 analog (paragraph 23). In other words, and incretin. Note that K20 has a fatty acid modification with a Glu linker (paragraph 27). The synthesis method was to synthesize the fragment containing K20 with an MTT protecting group (paragraph 66), followed by removing the MTT protecting group and adding the protected side chain modification (paragraph 77). This was then coupled with the remaining fragments to generate the finished polypeptide (paragraph 82). This reference discusses fragment based synthesis of a polypeptide with a side chain modification.
Therefore, it would be obvious to try the various combinations of fragments to find the best in terms of ease of synthesis, purity, and yield, as discussed by Bray. As Bray states that this is to be determined by trial and error (i.e. trying the possibilities to find the best), an artisan in this field would attempt this process with a reasonable expectation of success.
Furthermore, it would be obvious to generate the protected fragment containing K17 with the side chain modification of that amino acid on the fragment, as Leng et al used a similar protocol for synthesis of their incretin. As the side chain is similar in both cases (Glu attached to a fatty acid), an artisan in this field would attempt this synthesis with a reasonable expectation of success.
response to applicant’s arguments
Applicants have referred to the arguments made with respect to the rejection under 35 USC 103, above, which were discussed there.
fourth rejection
Claims 2, 4, 39, and 40 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 8 of U.S. Patent No. 12,365,716 in view of Bray (Nat. Rev. Drug Discov. (2003) 2 p587-593, cited by applicants) and Leng et al (CN 103864918). Note that Leng et al is in Chinese. A machine translation is relied upon, and references to locations in the document in this rejection refer to the machine translation.
Competing claim 38 describes a method of treating various disorders, comprising administering a polypeptide identical with SEQ ID 6 of the examined claims.
The difference between the competing claims and the examined claims is that the competing claims do not discuss synthesis of this sequence.
Bray discusses large scale manufacture of peptides (title). Synthesis of fragments is conducted on solid phase using acid sensitive resin to make protected fragments, which can then be coupled either on resin (solid phase) or in solution (p589, 1st column, 2nd paragraph). Fragment selection is crucial; selection is based on solubility, ease of synthesis, purity, yield, and the carboxyl terminus are considered, but the ideal fragments can only be determined by trial and error (p590, 3d column, 2nd paragraph). In the example of enfuviratide, the side chain protection is boc (for Lys residues), tBtu for Tyr, Thr, Ser, Glu, and Asp residues, and trt for Gln residues (fig 3, p591, right of page). Note that, because of the large number of reactions in peptide synthesis, a small difference in yield or purity at each step can make large differences in the final product (p592, 2nd column, 3d paragraph). This reference discusses scale up of peptide synthesis using fragment condensation methods.
Leng et al discusses the synthesis of liraglutide (title), a GLP-1 analog (paragraph 23). In other words, and incretin. Note that K20 has a fatty acid modification with a Glu linker (paragraph 27). The synthesis method was to synthesize the fragment containing K20 with an MTT protecting group (paragraph 66), followed by removing the MTT protecting group and adding the protected side chain modification (paragraph 77). This was then coupled with the remaining fragments to generate the finished polypeptide (paragraph 82). This reference discusses fragment based synthesis of a polypeptide with a side chain modification.
Therefore, it would be obvious to try the various combinations of fragments to find the best in terms of ease of synthesis, purity, and yield, as discussed by Bray. As Bray states that this is to be determined by trial and error (i.e. trying the possibilities to find the best), an artisan in this field would attempt this process with a reasonable expectation of success.
Furthermore, it would be obvious to generate the protected fragment containing K17 with the side chain modification of that amino acid on the fragment, as Leng et al used a similar protocol for synthesis of their incretin. As the side chain is similar in both cases (Glu attached to a fatty acid), an artisan in this field would attempt this synthesis with a reasonable expectation of success.
This is a provisional nonstatutory double patenting rejection.
response to applicant’s arguments
Applicants have referred to the arguments made with respect to the rejection under 35 USC 103, above, which were discussed there.
Conclusion
All claims are identical to or patentably indistinct from, or have unity of invention with claims in the application prior to the entry of the submission under 37 CFR 1.114 (that is, restriction (including a lack of unity of invention) would not be proper) and all claims could have been finally rejected on the grounds and art of record in the next Office action if they had been entered in the application prior to entry under 37 CFR 1.114. Accordingly, THIS ACTION IS MADE FINAL even though it is a first action after the filing of a request for continued examination and the submission under 37 CFR 1.114. See MPEP § 706.07(b). 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.
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/FRED H REYNOLDS/Primary Examiner, Art Unit 1658