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 .
Election/Restrictions and Claim Status
Applicants’ amendments and arguments filed 10/17/25 are acknowledged. Any objection or rejection from the 6/18/25 office action that is not addressed below is withdrawn based on the amendments and/or arguments.
Previously, Group 1 and the species of SEQ ID NO: 195 were elected.
Claims 53-55 require a different X16 than that of the elected species.
Claims to the elected species are rejected as set forth below. Any relevant art that was uncovered during the search for the elected species is cited herein in order to advance prosecution.
Claims 60-62 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 5/14/24.
Claims 53-55 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 5/14/24.
Claims 1-40, 46, 49-50 and 63 have been canceled.
Claims 41-45, 47-48, 51-52 and 56-59 are being examined.
Priority
The priority information is provided in the filing receipt dated 1/17/24.
Claim Rejections - 35 USC § 103
Claims were previously rejected based on the reference cited below. Since the claims have been amended the rejection is updated to correspond to the instant claims.
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.
Claim(s) 41-45, 47-48, 51-52 and 56-59 is/are rejected under 35 U.S.C. 103 as being unpatentable over Patel et al. (WO 2016/011208; as cited with IDS 7/11/23; ‘Patel’).
Patel teach peptide inhibitors of interleukin-23 (abstract). Patel teach pharmaceutical compositions (claim 44). Patel teach a disulfide bond between the Pen residues (claim 18 for example). Patel teach peptides of a generic formula (claim 1). Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11). Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). Patel teach that X16 is any amino acid (claim 1) specifically Gly (claim 28). Patel recognizes peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Patel teach the use of glycine to connect a C-terminal lysine (to form a peptide with length of 13 amino acids) that is used to conjugate to a polymeric moiety where the compound has activity in the ELISA assay (compound 305 on page 183). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11).
Patel does not teach a specific compound that reads on the instant claims.
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Patel based on the teachings and suggestions of Patel. Since Patel specifically teach peptides (claim 11, 3rd compound) that include Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 and provides specific patterns of preference and acceptable substitutions/insertions at positions X8 and X16 (see above) one would have been motivated to make such compounds. When Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 is modified at the X8 position as suggested (for example with Lys(Ac)) and Gly inserted at the X16 position as suggested the resulting compound comprises Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG. One would have been motivated to insert Gly at the X16 position since Patel teach peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Since Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33) and further teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090) and teach the use of modified or unnatural amino acids and specifically refers amino acids including those as shown in Table 1A (section 0097) (where Table 1A recites Lys(Ac)) (page 22)) one would have been motivated to use Lys(Ac) at X8. Further, Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example) so one would have been motivated to do such based on the express suggestions. One would have had a reasonable expectation of success based on the pattern of preference suggested by Patel. Further, Patel teach that the substitutions are made to achieve similar desired results (section 0097).The claims would have been obvious because the substitution/insertion of known elements would have yielded predictable results to one of ordinary skill in the art before the effective filing date.
In relation to the peptide of claims 41-45, 47-48, 51-52 and 56-59, Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG as discussed above is such that X4 is Pen, X5 is Gln, X6 is Thr, X7 is Trp, X8 is Lys(Ac), X9 is Pen, X10 is Phe[4-(2-aminoethoxy)], X11 is 2-Nal, X12 is alpha-MeLeu, X13 is Lys (Ac), X14 is Asn, X15 is Asn, X16 is Gly, R1 of claims 56-58 is Ac. Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11, compare instant X5).
Response to Arguments - 103
Applicant's arguments filed 10/17/25 have been fully considered but they are not persuasive with respect to the rejection set forth above.
Although applicants argue that the claims have been amended, the amended claims are addressed above.
Although applicants argue about the presence of an acylated residue at position 8, Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). MPEP 2123 recognizes that references are relevant for all that they contain including a broader disclosure and nonpreferred embodiments. MPEP 2123 II states that the ‘mere disclosure of more than one alternative does not constitute a teaching away from any of these alternatives because such disclosure does not criticize, discredit, or otherwise discourage the solution claimed’.
Double Patenting
Claims were previously rejected based on the patents and reference cited below. Since the claims have been amended, the rejections are updated to correspond to the instant claims
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 41-45, 47-48, 51-52 and 56-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-24 of U.S. Patent No. 9,624,268 (268 as cited with IDS 7/11/23) in view of Patel et al. (WO 2016/011208; as cited with IDS 7/11/23; ‘Patel’).
268 recites peptide inhibitors of interleukin-23 (claim 1). 268 recites pharmaceutical compositions (claim 24). 268 recites a disulfide bond between X4 (Pen) and X9 (Pen) (claim 3). 268 recites specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 5). 268 recites that X16 can be any amino acid (claim 1) specifically Gly (claim 11). 268 recites that X8 can be any amino acid (claim 1). 268 recites that X8 can be Lys (claim 14).
268 does not recite a specific compound that reads on the instant claims.
Patel teach peptide inhibitors of interleukin-23 (abstract). Patel teach pharmaceutical compositions (claim 44). Patel teach a disulfide bond between the Pen residues (claim 18 for example). Patel teach peptides of a generic formula (claim 1). Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11). Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). Patel teach that X16 is any amino acid (claim 1) specifically Gly (claim 28). Patel recognizes peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Patel teach the use of glycine to connect a C-terminal lysine (to form a peptide with length of 13 amino acids) that is used to conjugate to a polymeric moiety where the compound has activity in the ELISA assay (compound 305 on page 183). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 268 based on the teachings and suggestions of 268. Further, Patel teach the same peptide (3rd compound of claim 11) as the 3rd compound of claim 5 of 268. Thus one would have been motivated to incorporate the known teachings related to this class of peptides. Since 268 and Patel specifically teach peptides (claim 11, 3rd compound) that include Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 and provides specific patterns of preference and acceptable substitutions/insertions at positions X8 and X16 (see above) one would have been motivated to make such compounds. When Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 is modified at the X8 position as suggested (Lys(Ac)) and Gly inserted at the X16 position as suggested the resulting compound comprises Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG. One would have been motivated to insert Gly at the X16 position since Patel teach peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Since Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Gln or Lys (claims 24 and 33) and further teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090) and teach the use of modified or unnatural amino acids and specifically refers to alpha-methyl amino acids (section 0097) including those as shown in Table 1A (section 0097) (where Table 1A recites Lys(Ac) (page 22)) one would have been motivated to use Lys(Ac) at X8. Further, Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example) so one would have been motivated to do such based on the express suggestions. One would have had a reasonable expectation of success based on the pattern of preference suggested by Patel. Further, Patel teach that the substitutions are made to achieve similar desired results (section 0097). The claims would have been obvious because the substitution/insertion of known elements would have yielded predictable results to one of ordinary skill in the art before the effective filing date.
In relation to the peptide of claims 41-45, 47-48, 51-52 and 56-59, Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG as discussed above is such that X4 is Pen, X5 is Gln, X6 is Thr, X7 is Trp, X8 is Lys(Ac), X9 is Pen, X10 is Phe[4-(2-aminoethoxy)], X11 is 2-Nal, X12 is alpha-MeLeu, X13 is Lys (Ac), X14 is Asn, X15 is Asn, X16 is Gly, R1 of claims 56-58 is Ac. Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example).
Claims 41-45, 47-48, 51-52 and 56-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-22 of U.S. Patent No. 10,196,424 (424 as cited with IDS 7/11/23) in view of Patel et al. (WO 2016/011208; as cited with IDS 7/11/23; ‘Patel’).
424 recites peptide inhibitors of interleukin-23 (claim 1). 424 recites a disulfide bond between X4 (Pen) and X9 (Pen) (claim 7). 424 recites specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 15). 424 recites that X16 can be any amino acid (claim 1). 424 recites that X8 can be any amino acid (claim 1). 424 recites that X8 can be Lys (claim 14).
424 does not recite a specific compound that reads on the instant claims.
Patel teach peptide inhibitors of interleukin-23 (abstract). Patel teach pharmaceutical compositions (claim 44). Patel teach a disulfide bond between the Pen residues (claim 18 for example). Patel teach peptides of a generic formula (claim 1). Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11). Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). Patel teach that X16 is any amino acid (claim 1) specifically Gly (claim 28). Patel recognizes peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Patel teach the use of glycine to connect a C-terminal lysine (to form a peptide with length of 13 amino acids) that is used to conjugate to a polymeric moiety where the compound has activity in the ELISA assay (compound 305 on page 183). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 424 based on the teachings and suggestions of 424. Further, Patel teach the same peptide (3rd compound of claim 11) as the 3rd compound of claim 15 of 424. Thus one would have been motivated to incorporate the known teachings related to this class of peptides. Since 424 and Patel specifically teach peptides (claim 11, 3rd compound) that include Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 and provides specific patterns of preference and acceptable substitutions/insertions at positions X8 and X16 (see above) one would have been motivated to make such compounds. When Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 is modified at the X8 position as suggested (Lys(Ac)) and Gly inserted at the X16 position as suggested the resulting compound comprises Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG. One would have been motivated to insert Gly at the X16 position since Patel teach peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Since Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33) and further teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090) and teach the use of modified or unnatural amino acids and specifically refers to amino acids (section 0097) including those as shown in Table 1A (section 0097) (where Table 1A recites Lys(Ac) (page 22)) one would have been motivated to use Lys(Ac) at X8. Further, Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example) so one would have been motivated to do such based on the express suggestions. One would have had a reasonable expectation of success based on the pattern of preference suggested by Patel. Further, Patel teach that the substitutions are made to achieve similar desired results (section 0097). The claims would have been obvious because the substitution/insertion of known elements would have yielded predictable results to one of ordinary skill in the art before the effective filing date.
In relation to the peptide of claims 41-45, 47-48, 51-52 and 56-59, Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG as discussed above is such that X4 is Pen, X5 is Gln, X6 is Thr, X7 is Trp, X8 is Lys(Ac), X9 is Pen, X10 is Phe[4-(2-aminoethoxy), X11 is 2-Nal, X12 is alpha-MeLeu, X13 is Lys (Ac), X14 is Asn, X15 is Asn, X16 is Gly, R1 of claims 56-58 is Ac. Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example).
Claims 41-45, 47-48, 51-52 and 56-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 10,023,614 (614 as cited with IDS 7/11/23) in view of Patel et al. (WO 2016/011208; as cited with IDS 7/11/23; ‘Patel’).
614 recites peptide inhibitors of interleukin-23 (claim 1). 614 recites a disulfide bond between X4 (Pen) and X9 (Pen) (claim 1). 614 recites specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (claim 7). 614 recites that X16 can be any amino acid (claim 1).
614 does not recite a specific compound that reads on the instant claims.
Patel teach peptide inhibitors of interleukin-23 (abstract). Patel teach pharmaceutical compositions (claim 44). Patel teach a disulfide bond between the Pen residues (claim 18 for example). Patel teach peptides of a generic formula (claim 1). Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11). Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). Patel teach that X16 is any amino acid (claim 1) specifically Gly (claim 28). Patel recognizes peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Patel teach the use of glycine to connect a C-terminal lysine (to form a peptide with length of 13 amino acids) that is used to conjugate to a polymeric moiety where the compound has activity in the ELISA assay (compound 305 on page 183). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 614 based on the teachings and suggestions of 614. Further, Patel teach the same peptide (3rd compound of claim 11) as the compound of claim 7 of 614. Thus one would have been motivated to incorporate the known teachings related to this class of peptides. Since 614 and Patel specifically teach peptides (claim 11, 3rd compound) that include Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 and provides specific patterns of preference and acceptable substitutions/insertions at positions X8 and X16 (see above) one would have been motivated to make such compounds. When Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 is modified at the X8 position as suggested (Lys(Ac)) and Gly inserted at the X16 position as suggested the resulting compound comprises Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG. One would have been motivated to insert Gly at the X16 position since Patel teach peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Since Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33) and further teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090) and teach the use of modified or unnatural amino acids and specifically refers to amino acids (section 0097) including those as shown in Table 1A (section 0097) (where Table 1A recites Lys(Ac) (page 22)) one would have been motivated to use Lys(Ac) at X8. Further, Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example) so one would have been motivated to do such based on the express suggestions. One would have had a reasonable expectation of success based on the pattern of preference suggested by Patel. Further, Patel teach that the substitutions are made to achieve similar desired results (section 0097). The claims would have been obvious because the substitution/insertion of known elements would have yielded predictable results to one of ordinary skill in the art before the effective filing date.
In relation to the peptide of claims 41-45, 47-48, 51-52 and 56-59, Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG as discussed above is such that X4 is Pen, X5 is Gln, X6 is Thr, X7 is Trp, X8 is Lys(Ac), X9 is Pen, X10 is Phe[4-(2-aminoethoxy)], X11 is 2-Nal, X12 is alpha-MeLeu, X13 is Lys (Ac), X14 is Asn, X15 is Asn, X16 is Gly, R1 of claims 56-58 is Ac. Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example).
Claims 41-45, 47-48, 51-52 and 56-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 10,787,490 (490 as cited with IDS 7/11/23) in view of Patel et al. (WO 2016/011208; as cited with IDS 7/11/23; ‘Patel’).
490 recites peptide inhibitors of interleukin-23 (claim 1). 490 recites specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-[Phe[ 4-CONH2]-[2-Nal]-[a-MeLys(Ac) ]-[Lys(Ac)]-NN-NH2 (claim 1 compound 3).
490 does not recite a specific compound that reads on the instant claims.
Patel teach peptide inhibitors of interleukin-23 (abstract). Patel teach pharmaceutical compositions (claim 44). Patel teach a disulfide bond between the Pen residues (claim 18 for example). Patel teach peptides of a generic formula (claim 1). Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11). Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). Patel teach that X16 is any amino acid (claim 1) specifically Gly (claim 28). Patel recognizes peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Patel teach the use of glycine to connect a C-terminal lysine (to form a peptide with length of 13 amino acids) that is used to conjugate to a polymeric moiety where the compound has activity in the ELISA assay (compound 305 on page 183). In addition, Patel teach that the residue after the first Pen can be Q or N (claim 11).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 490 based on the teachings and suggestions of 490. Further, Patel teach similar peptides (3rd-4th compound of claim 11) as the 3rd compound of claim 1 of 490. Thus one would have been motivated to incorporate the known teachings related to this class of peptides. Since 490 and Patel specifically teach similar peptides and provides specific patterns of preference and acceptable substitutions/insertions at positions X8 and X16 (see above) one would have been motivated to make such compounds. When Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-CONH2]-[2-Nal]-[a-MeLys(Ac) ]-[Lys(Ac)]-NN-NH2 is modified at the X8 position as suggested (Lys(Ac)) and X12 (alphaMeLeu) and Gly inserted at the X16 position as suggested the resulting compound comprises Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-[Phe[ 4-CONH2]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NNG. One would have been motivated to insert Gly at the X16 position since Patel teach peptides with polymeric moieties conjugated for improved stability and half-life (section 00533) where a spacer is present (section 00534). Since Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33) and further teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090) and teach the use of modified or unnatural amino acids and specifically refers to amino acids (section 0097) including those as shown in Table 1A (section 0097) (where Table 1A recites Lys(Ac) (page 22)) one would have been motivated to use Lys(Ac) at X8. Patel teach specific compounds including Ac-[Pen ]-Q-T-W-Q-[Pen]-Phe[ 4-(2-aminoethoxy)]-[2-Nal]-[alphaMeLeu]-[Lys(Ac)]-NN-NH2 (3rd compound of claim 11) which include alpha-MeLeu at position X12. Further, Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example) so one would have been motivated to do such based on the express suggestions. One would have had a reasonable expectation of success based on the pattern of preference suggested by Patel. Further, Patel teach that the substitutions are made to achieve similar desired results (section 0097). The claims would have been obvious because the substitution/insertion of known elements would have yielded predictable results to one of ordinary skill in the art before the effective filing date.
In relation to the peptide of claims 41-45, 47-48, 51-52 and 56-59, Ac-[Pen ]-Q-T-W-[Lys(Ac)]-[Pen]-Phe[ 4-CONH2]-[2-Nal]-[alpha-MeLeu ]-[Lys(Ac)]-NNG as discussed above is such that X4 is Pen, X5 is Gln, X6 is Thr, X7 is Trp, X8 is Lys(Ac), X9 is Pen, X10 is Phe(4-CONH2), X11 is 2-Nal, X12 is alpha-MeLeu, X13 is Lys (Ac), X14 is Asn, X15 is Asn, X16 is Gly, R1 of claims 56-58 is Ac. Patel teach pharmaceutical compositions (claim 44) and teach a disulfide bond between the Pen residues (claim 18 for example).
Response to Arguments – double patenting
Applicant's arguments filed 10/17/25 have been fully considered but they are not persuasive.
Although applicants argue that the claims have been amended, the amended claims are addressed above.
Although applicants argue about the presence of an acylated residue at position 8, Patel recognizes that X8 can be any amino acid (claim 1) and specifically teach that X8 is Lys (claims 24 and 33). Patel teach that the peptides can be present with enzymes that cleave the peptides (section 0089) and that reduced susceptibility to proteases is desired (section 0090). Patel teach the use of modified or unnatural amino acids and specifically and teach that the peptide inhibitor can include one of the amino acids shown in Table 1A (section 0097) where Table 1A recites Lys(Ac) (page 22). Patel teach that the substitutions are made to achieve similar desired results (section 0097). MPEP 2123 recognizes that references are relevant for all that they contain including a broader disclosure and nonpreferred embodiments. MPEP 2123 II states that the ‘mere disclosure of more than one alternative does not constitute a teaching away from any of these alternatives because such disclosure does not criticize, discredit, or otherwise discourage the solution claimed’.
Although applicants argue about the use of hindsight, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Conclusion
Applicant's amendment necessitated any new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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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RONALD T. NIEBAUER
Primary Examiner
Art Unit 1658
/RONALD T NIEBAUER/Examiner, Art Unit 1658