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 11/3/25 are acknowledged. Any objection or rejection from the 8/1/25 office action that is not addressed below is withdrawn based on the amendments.
Previously, Group 1 and the compound 3-PhPh-AQTGTGKT were elected.
Claims 14-15 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 6/27/25.
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.
Since the elected species is such that X is 3PhPh, claims 9, 11 and 13 are drawn to non-elected species.
Claims 9, 11 and 13 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 6/27/25.
Claims 3-8, 10 and 16-17 have been canceled.
Claims 1-2 and 12 are being examined.
Priority
The priority information is found in the filing receipt of 2/15/23.
Claim Rejections - 35 USC § 103
Claims were previously rejected based on the references cited below. Since the claims have been amended the rejections are updated to correspond to the instant claims.
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.
Claim(s) 1-2 is/are rejected under 35 U.S.C. 103 as being unpatentable over Yeon et al. (NPL cite 2 of IDS of 10/21/22; ‘Yeon’) in view of Sorolla et al. (first cited 5/8/25; ‘Sorolla’).
Yeon teach the peptide AQTGTGKT and states that the results present evidence that the peptide could overcome resistance of non-small cell lung cancers to anti-cancer drugs (abstract). Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last complete paragraph for example). Yeon teach the inclusion of protease inhibitors (page 3 first paragraph).
Yeon does not teach the X group on the peptide as in instant claims 1-2.
Sorolla teach peptides used in cancer treatments (abstract). Sorolla teach that a problem with peptides is their sensitivity to proteases which reduce their half-life (page 1179 first paragraph). Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Yeon because Yeon teach the peptide AQTGTGKT and states that the results present evidence that the peptide could overcome resistance of non-small cell lung cancers to anti-cancer drugs (abstract). Since Yeon teach beneficial results with AQTGTGKT and suggest uses of the peptide, one would have been motivated to prepare in an appropriate form. Sorolla teach that a problem with peptides is their sensitivity to proteases which reduce their half-life (page 1179 first paragraph). Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). Thus, one would have been motivated to acetylate the N-terminus of AQTGTGKT. Since Yeon suggest uses of the peptide and the peptide in various assays (page 3 last paragraph for example) one would have been motivated to make compositions with the peptide. One would have had a reasonable expectation of success since Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last complete paragraph for example).
In relation to the peptide of claims 1-2, Yeon teach the peptide AQTGTGKT (abstract).
In relation to the X group of claims 1-2, Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph) where the acetyl group is CH3-C(O)- (the 2nd X group of claims 1-2).
In relation to the composition of claim 2, Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last paragraph for example).
Claim(s) 1-2 and 12 is/are rejected under 35 U.S.C. 103 as being unpatentable over Yeon et al. (NPL cite 2 of IDS of 10/21/22; ‘Yeon’) in view of Ben-Sasson (US 2002/0028772) in view of Yu et al. (US 2004/0229882; ‘Yu’).
Yeon teach the peptide AQTGTGKT and states that the results present evidence that the peptide could overcome resistance of non-small cell lung cancers to anti-cancer drugs (abstract). Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last complete paragraph for example). Yeon teach the inclusion of protease inhibitors (page 3 first paragraph).
Yeon does not teach the X group on the peptide as in instant claims 1-2.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Yu also teach additional dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0276). Yu teach compound 151 which includes a specific R19 group (3-PhPh) (page 37).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Yeon because Yeon teach the peptide AQTGTGKT and states that the results present evidence that the peptide could overcome resistance of non-small cell lung cancers to anti-cancer drugs (abstract). Since Yeon teach beneficial results with AQTGTGKT and suggest uses of the peptide, one would have been motivated to prepare in an appropriate form. Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035) and specific benefits including increased half-lives (section 0055). Since Ben-Sasson recites biphenyl as a protecting group (section 0055) one would have been motivated to use the known configurations as taught by Yu. Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Thus, one would have been motivated to include the 3-PhPh-C(O)- group at the N-terminus of AQTGTGKT. Since Yeon suggest uses of the peptide and the peptide in various assays (page 3 last paragraph for example) one would have been motivated to make compositions with the peptide. One would have had a reasonable expectation of success since Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last paragraph for example).
In relation to the peptide of claims 1-2, Yeon teach the peptide AQTGTGKT (abstract).
In relation to the X group of claims 1-2 and 12, Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). The 3-PhPh-C(O)- group corresponds to the 3rd X group of claims 1-2.
In relation to the composition of claim 2, Yeon teach that the peptide was synthesized and purified (page 2 section ‘Peptides’) and used in various assays (page 3 last paragraph for example).
In relation to the functionality recited in claim 12, the prior art suggest a compound as claimed so it would function as claimed. Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Response to Arguments - 103
Applicant's arguments filed 11/3/25 have been fully considered but they are not persuasive with respect to the rejections set forth above.
Although applicants argue that there is no reason to modify the peptide AQTGTGKT, Yeon teach the peptide AQTGTGKT and states that the results present evidence that the peptide could overcome resistance of non-small cell lung cancers to anti-cancer drugs (abstract). Since Yeon teach beneficial results with AQTGTGKT and suggest uses of the peptide, one would have been motivated to prepare in an appropriate form. Sorolla teach that a problem with peptides is their sensitivity to proteases which reduce their half-life (page 1179 first paragraph). Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). Thus, one would have been motivated to acetylate the N-terminus of AQTGTGKT. Further, Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035) and specific benefits including increased half-lives (section 0055). Since Ben-Sasson recites biphenyl as a protecting group (section 0055) one would have been motivated to use the known configurations as taught by Yu. Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Thus, one would have been motivated to include the 3-PhPh-C(O)- group at the N-terminus of AQTGTGKT.
Although applicants argue about the references individually, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). The rejections set forth above are multiple reference 103 rejections and as such any single reference does not necessarily anticipate the claims.
Although applicants argue that certain references do not provide experimental evidence, MPEP 2123 I recognizes that a reference may be relied upon for all that it would have reasonably suggested to one having ordinary skill in the art. Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). The first page of Sorolla states ‘REVIEW ARTICLE’ and as such does not necessarily provide new data but reviews known data. One would have been motivated by the express statements provided by the references as discussed in detail in the rejections.
Although applicants argue about alleged marked improvements in stability, MPEP 716.02(c) recognizes that expected beneficial results are evidence of obviousness and MPEP 716.02 states that the issue is whether the properties differ to an extent that the difference is really unexpected.
Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). Thus, based on the known properties, an improved half-life for Ac-AQTGTGKT as compared to AQTGTGKT is not necessarily unexpected.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055). Thus, based on the known properties, an improved half-life for phenyl (Ph- AQTGTGKT) or substituted phenyl (4-PhPh, 3-PhPh, 4-MeOPh, 2-PhPh and naphthyl) as compared to AQTGTGKT is not necessarily unexpected.
Although applicants argue that PEGylation and lipidation type modifications were found that were not markedly different, MPEP 716.02(b) states that the burden is on the applicant to establish results are in fact unexpected and of statistical significance and the burden is on the applicant to explain the data. The compound structures on page 11 of the 11/3/25 reply are unclear. 3 of the compounds are named ‘1kPEG-AQTGTGKT’. The actual data provided recites a lipidated-AQTGTGKT with a Human t/2 of 2.5 min and a 40kDa PEG-AQTGTGKT with a Human t/2 of 2.7 min as compared to a Human t/2 of <1 min for AQTGTGKT. It is unclear why a change from <1 to 2.5 or 2.7 is deemed not markedly different. The statistical significance of the data has not been provided.
It is also noted that applicants have previously stated on the record that ‘The differences in the substituent group X represent structural variations and do not affect the fundamental therapeutic action of the compounds. The structural modifications are predictable variants’ (page 9 of 6/27/25 reply; emphasis added).
Although applicants argue about teachings from an Eldeeb et al. reference, such reference does recognize the role of steric shielding (page 6 paragraph connecting columns 1-2). Sorolla refers to peptides sensitivity to proteases and teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). Although Eldeeb et al. teach that yeast for example (see figure 4) might have additional pathways for protein degradation, the teachings of Eldeeb do not discredit acetylation helping reduce sensitivity to proteases.
Although applicants argue about thiol containing peptides and a Fontaine reference, the instant peptides do not contain a thiol or cysteine so the relevance is unclear.
Although applicants argue about reference 3, no copy of such reference has been provided and such reference has not been cited on an IDS. The excerpt picture provided by the applicant is not legible.
Although applicants argue about superior tumor retention (pages 14-15 of the reply), MPEP 716.02(b) states that the burden is on the applicant to establish results are in fact unexpected and of statistical significance and the burden is on the applicant to explain the data. The picture shown on page 14 of the 11/3/25 reply is not legible and the details of the experiment have not been set forth. Further, the conclusion as provided by the applicants refers to the peptides ‘remain longer’.
Sorolla teach that a common modification to enhance peptide stability is acetylation of the N-terminus (page 1179 first paragraph). Thus, based on the known properties, an improved half-life (or a peptide remaining longer) for an acetylated peptide is not necessarily unexpected.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055). Thus, based on the known properties, an improved half-life (or a peptide remaining longer) for phenyl (Ph- AQTGTGKT) or substituted phenyl (4-PhPh, 3-PhPh, 4-MeOPh, 2-PhPh and naphthyl) as compared to AQTGTGKT is not necessarily unexpected.
In summary, there are inadequate facts to establish unexpected results. As discussed in detail above, the prior art recognizes certain modifications that are suggested to improve stability and half-life. Expected beneficial results are evidence of obviousness.
Although applicants argue that there are numerous alternatives, Sorolla teach: “The most common structural modifications adopted to enhance peptide stability are chemical modifications in the N- and C-termini of the peptide backbone (e.g., acetylation of the Nterminus)’ (page 1179 first paragraph). Since N-terminal acetylation is described as the most common one would have been motivated to modify in such fashion. Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055). Further, Yu teach compound 151 which includes a specific R19 group (3-PhPh) (page 37). Thus, one would have been motivated by the teachings and examples of the references.
Double Patenting
Claims were previously rejected based on the applications/patents and references 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 1-2 and 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 30-48 of copending Application No. 18550775 (reference application; ‘775’). Although the claims at issue are not identical, they are not patentably distinct from each other.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
775 recites compositions comprising the compound X-AQTGTGKT where a finite number of X residues are recited (claim 48).
In relation to the peptide of claims 1-2, 775 recites compositions comprising the compound X-AQTGTGKT (claim 48).
In relation to the X group of claims 1-2 and 12, 775 recites compositions comprising the compound X-AQTGTGKT (claim 48 including the 3rd option for X; compare MPEP 2131.02 III 2nd-3rd paragraph).
In relation to the composition of claim 2, 775 recites compositions (claim 48).
In relation to the functionality recited in claim 12, the prior art teach a compound as claimed so it would function as claimed.
Claims 1-2 and 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4-6, 8-18, 20, 22-23 and 25 of copending Application No. 18692883 (883) in view of Yeon et al. (NPL cite 2 of IDS of 10/21/22; ‘Yeon’) in view of Ben-Sasson (US 2002/0028772) in view of Yu et al. (US 2004/0229882; ‘Yu’).
This is a provisional nonstatutory double patenting rejection.
883 teach the peptide AQTGTGKT (claim 2) and refers to compositions (claim 25) and teach methods of administering (claim 1). 883 suggests an X group including an acylated modified phenyl group (claim 2 chemical formula 3)
883 does not recite a specific X group on the peptide as in instant claims 1-2.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Yu also teach additional dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0276). Yu teach compound 151 which includes a specific R19 group (3-PhPh) (page 37).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 883 because 883 teach the peptide AQTGTGKT and specifically suggest X groups on the peptide. Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035) and specific benefits including increased half-lives (section 0055). Since Ben-Sasson recites biphenyl as a protecting group (section 0055) one would have been motivated to use the known configurations as taught by Yu. Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Thus, one would have been motivated to include the 3-PhPh-C(O)- group at the N-terminus of AQTGTGKT. Since 883 teach compositions (claim 25) one would have been motivated to make compositions with the peptide. One would have had a reasonable expectation of success since Ben-Sasson teach peptides can be produced using known techniques (section 0067).
In relation to the peptide of claims 1-2, 883 teach the peptide AQTGTGKT (claim 2)
In relation to the X group of claims 1-2 and 12, Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). The 3-PhPh-C(O)- group corresponds to the 3rd X group of claims 1-2.
In relation to the composition of claim 2, 883 teach the peptide AQTGTGKT and compositions thereof (claim 2).
In relation to the functionality recited in claim 12, the prior art suggest a compound as claimed so it would function as claimed. Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Claims 1-2 and 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 of U.S. Patent No. 10,233,221 (221) in view of Yeon et al. (NPL cite 2 of IDS of 10/21/22; ‘Yeon’) in view of Ben-Sasson (US 2002/0028772) in view of Yu et al. (US 2004/0229882; ‘Yu’).
221 teach the peptide AQTGTGKT and compositions thereof (claim 1) and teach methods of treating (claim 5).
221 does not teach the X group on the peptide as in instant claims 1-2.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Yu also teach additional dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0276). Yu teach compound 151 which includes a specific R19 group (3-PhPh) (page 37).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 221 because Yeon teach the peptide AQTGTGKT and teach uses thereof (claims 1 and 5). Since 221 suggest uses of the peptide, one would have been motivated to prepare in an appropriate form. Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035) and specific benefits including increased half-lives (section 0055). Since Ben-Sasson recites biphenyl as a protecting group (section 0055) one would have been motivated to use the known configurations as taught by Yu. Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Thus, one would have been motivated to include the 3-PhPh-C(O)- group at the N-terminus of AQTGTGKT. Since 221 teach compositions (claim 1) one would have been motivated to make compositions with the peptide. One would have had a reasonable expectation of success since Ben-Sasson teach peptides can be produced using known techniques (section 0067).
In relation to the peptide of claims 1-2, 221 teach the peptide AQTGTGKT (claim 1)
In relation to the X group of claims 1-2 and 12, Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). The 3-PhPh-C(O)- group corresponds to the 2nd X group of claims 1-2.
In relation to the composition of claim 2, 221 teach the peptide AQTGTGKT and compositions thereof (claim 1).
In relation to the functionality recited in claim 12, the prior art suggest a compound as claimed so it would function as claimed. Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Claims 1-2 and 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 10,239,924 (924) in view of Yeon et al. (NPL cite 2 of IDS of 10/21/22; ‘Yeon’) in view of Ben-Sasson (US 2002/0028772) in view of Yu et al. (US 2004/0229882; ‘Yu’).
924 teach the peptide AQTGTGKT (claim 1) and teach methods of administering (claim 1).
924 does not teach the X group on the peptide as in instant claims 1-2.
Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035). Ben-Sasson teach that protecting groups can facilitate transport of a peptide into a cell (section 0035). Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Yu also teach additional dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0276). Yu teach compound 151 which includes a specific R19 group (3-PhPh) (page 37).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 924 because Yeon teach the peptide AQTGTGKT and teach uses thereof (claims 1 and 9). Since 924 suggest uses of the peptide, one would have been motivated to prepare in an appropriate form. Ben-Sasson teach the use of N-terminal protecting groups including acyl groups where the acyl group can be a substituted phenyl (section 0035) and specific benefits including increased half-lives (section 0055). Since Ben-Sasson recites biphenyl as a protecting group (section 0055) one would have been motivated to use the known configurations as taught by Yu. Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). Thus, one would have been motivated to include the 3-PhPh-C(O)- group at the N-terminus of AQTGTGKT. One would have had a reasonable expectation of success since Ben-Sasson teach peptides can be produced using known techniques (section 0067).
In relation to the peptide of claims 1-2, 924 teach the peptide AQTGTGKT (claim 1)
In relation to the X group of claims 1-2 and 12, Yu teach dipeptide compounds where the N-terminal amino acid includes an acyl group (R19-C(O)-) (section 0274). Yu teach compound 96 which includes a specific R19 group (3-PhPh) (page 34). The 3-PhPh-C(O)- group corresponds to the 2nd X group of claims 1-2.
In relation to the composition of claim 2, 924 teach methods of administering (claim 1) so one would have been motivated to include in an appropriate form.
In relation to the functionality recited in claim 12, the prior art suggest a compound as claimed so it would function as claimed. Ben-Sasson teach protecting groups to allow for longer biological half-lives and specifically recites biphenyl as a protecting group (section 0055).
Response to Arguments – double patenting
Applicant's arguments filed 11/3/25 have been fully considered but they are not persuasive with respect to the rejections set forth above.
Although applicants refer to arguments above, those arguments have been considered and are not found persuasive.
Although applicants argue about a situation in which the double patenting rejections are the only remaining rejections, claims are currently rejected under 103 so that situation does not currently exist.
Although applicants argue about Yeon, Ben-Sasson and Yu, the first double patenting rejection is based solely on copending Application No. 18550775.
Conclusion
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 RONALD T NIEBAUER whose telephone number is (571)270-3059. The examiner can normally be reached M - F 6:30 - 2:30 EST.
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RONALD T. NIEBAUER
Primary Examiner
Art Unit 1658
/RONALD T NIEBAUER/Examiner, Art Unit 1658