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 .
Claim Status
Claims 1-2 and 6-10 are pending.
Claim 1 is currently amended and claims 6-10 are new.
Claims 3-5 were cancelled.
Claims 1-2 and 6-10 have been examined.
Priority
This application is a 371 of PCT/JP2020/027261 filed on 07/13/2020 with foreign priority of JAPAN 2019-137126 filed on 07/25/2019.
Withdrawn Objection and Rejection
All objection and rejections are withdrawn because the amendments to claim 1 overcome the objection and rejections of record.
New Ground of Rejection
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 10 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 10 is drawn to the peptide mixture of the agent consisting of Gly-Pro (MW= 172.18 g/mol) and Glu-Hyp-Gly (MW= 317.30 g/mol), but the peptide mixture does not further limit the average molecular weight from 450 Da to 5,000 Da in claim 1 because neither Gly-Pro nor Glu-Hyp-Gly has molecular weight > 450 Da.
Furthermore, the agent consisting of Gly-Pro and Glu-Hyp-Gly (% of Gly-Pro + % of Glu-Hyp-Gly = 100%) in claim 10 fails to further limit the subject matter of the amount of Gly-Pro in an amount of from 1,159 ppm (0.1159% by weight) to 26,387 ppm (2.638% by weight) and Glu-Hyp-Gly in an amount of from 4 ppm (0.0004% by weight) to 24 ppm (0.0024% by weight) in claim 1.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Modified Rejection
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.
Claims 1-2 and 6-9 are rejected under 35 U.S.C. 103 as being unpatentable over Koizumi et al. (US 2016/0082087 A1, previously cited 1/24/2025) in view of Lee et al. (Biosci Biotechnol Biochem. 2019 Jun;83(6):1146-1156) and JP2006151847A (referred as JP2006).
The broadest reasonable interpretation of claim 1 is drawn to an agent comprising a peptide mixture comprising
a peptide consisting of the amino acid sequence Gly-Pro or a salt thereof in an amount of from 1,159 ppm (0.1159 %) to 26,387 ppm (2.638 %) and
a tripeptide peptide consisting of the amino acid sequence of Glu-Hyp-Gly or a salt thereof in an amount of from 4 ppm (0.0004 %) to 24 ppm (0.0024 %)
a weight average molecular weight of from 450 Da to 5,000 Da.
The intended use of an aging progression suppressing agent does not further add a limitation to the ingredients of the claimed agent. A composition meets all limitations (i)-(iii) would satisfy the claim.
Koizumi et al. teach a collagen peptide mixture in an agent comprising a dipeptide of Gly-Pro and a tripeptide of Glu-Hyp-Gly [0030]. Koizumi et al. teach the collagen peptide mixture produced by hydrolyzing collagen/gelatin via two or more protease digestion known in the art [0033]. Koizumi et al. teach the collagen peptide mixture used to suppress pigmentation, promote expression of transglutaminase 1, involucrin, keratin 10 and filaggrin, and thus promote epidermal metabolism to promote turnover of the skin [0027-0028]. Koizumi et al. suggest dose of the peptides is a result effective variable depending on condition and body weight of the subject, kind of the com pound, an administration route and so on [0039]. Koizumi et al. further teach the agent of collagen peptides mixed in beverage or food [0038]. For 1 L of beverage comprising 0.1 to 2000 mg of individual collagen peptides, each peptide can be optimized in a suggested range from 0.1 ppm to 2000 ppm (1 ppm = 1 mg/L) [0039]. Lee et al. is cited to show Gly-Pro derived from collagen known to be capable of protecting against UVB-induced skin aging (Title; p1150, col 2). Thus, one of ordinary skill in the art would expect to optionally add more dipeptide of Gly-Pro to Koizumi’s collagen peptide mixture (beyond 2000 ppm) to optimize bioactivity for protecting skin aging, reading on the limitation (i).
With respect to the limitation (ii), For 1 L of beverage comprising 0.1 to 2000 mg of individual collagen peptides, each peptide can be optimized in a suggested range from 0.1 ppm to 2000 ppm (1 ppm = 1 mg/L), but can also out of the range [0039]. Koizumi et al. further suggest the collagen peptide mixture comprising a tripeptide of Glu-Hyp-Gly. In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990). See MPEP 2144.05(I).
Koizumi et al. teach the collagen peptide mixture produced by hydrolyzing gelatin via two or more protease digestion known in the art [0033], but do not specify the average molecular weight of collagen peptides.
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Similarly, JP2006 teaches “Collagen peptide composition, method for producing the same and cosmetic composition” (Title). JP2006 teaches collagen protein hydrolysate comprising 60 to 100 wt.% of peptides having a molecular weight of from 400 to less than 3,000, less than 25 wt.% of peptides of a molecular weight of less than 400 and less than 15 wt.% of peptides of a molecular weight of more than 3,000 (p14, Abstract, claim 1). The estimated average molecular weight is 1,570 Da as calculated by 3000 x 15% + [(400+3000)÷2] x 60% + 400 x 25% shown as follows, reading on the limitation (iii).
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine Koizumi et al. and Lee et al. because (i) Koizumi et al. teach a collagen peptide mixture comprising a dipeptide of Gly-Pro and a tripeptide of Glu-Hyp-Gly [0030] and (b) Lee et al. show Gly-Pro derived from collagen known to be capable of protecting against UVB-induced skin aging (Title; p1150, col 2). The combination would have reasonable expectation of success because both references teach a bioactive dipeptide of Gly-Pro.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Koizumi et al. and Lee et al. with (ii) JP2006 because (a) Koizumi et al. teach a collagen peptide mixture produced by hydrolyzing collagen/gelatin via two or more protease digestion known in the art [0033] for therapeutic and cosmetic use [0037] via oral administration [0038] and (b) JP2006 teaches collagen protein hydrolysate comprising 60 to 100 wt.% of peptides having a molecular weight of from 400 to less than 3,000, less than 25 wt.% of peptides of a molecular weight of less than 400 and less than 15 wt.% of peptides of a molecular weight of more than 3,000 for cosmetic use (p14, Abstract, claim 1). The combination would have reasonable expectation of success because both Koizumi et al. and JP2006 teach the use of collagen peptide hydrolysate as a pharmaceutical/cosmetic agent.
With respect to claim 2, Koizumi et al. teach a dipeptide of Gly-Pro and a tripeptide of Glu-Hyp-Gly from collagen [0030].
With respect to claim 6, Koizumi et al. further teach the agent of collagen peptides mixed in beverage or food [0038].
With respect to claims 7-9, Koizumi et al. further teach the agent of collagen peptides mixed in beverage or food [0038]. Koizumi et al. teach the dose of administered peptide is a result effective variable depending on condition and body weight of the subject, kind of the com pound, an administration route and so on [0039]. For 1 L of beverage comprising 0.1 to 2000 mg of individual collagen peptides, each peptide can be optimized in a suggested range from 0.1 ppm to 2000 ppm (1 ppm = 1 mg/L) [0039]. Lee et al. is cited to show Gly-Pro derived from collagen known to be capable of protecting against UVB-induced skin aging (Title; p1150, col 2). Thus, one of ordinary skill in the art would expect to optionally add more dipeptide of Gly-Pro to Koizumi’s collagen peptide mixture (beyond 2000 ppm) to optimize bioactivity for protecting skin aging. Koizumi et al. further suggest the collagen peptide mixture comprising a tripeptide of Glu-Hyp-Gly. In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990). See MPEP 2144.05(I).
Response to Arguments
Applicant's arguments filed 12/31/2025 have been fully considered but they are not persuasive because the arguments do not apply to the modified rejection based on Koizumi et al. (US 2016/0082087 A1) in view of Lee et al. (Bioscience, Biotechnology, and Biochemistry, 83:6, 1146-1156) and JP2006151847A (referred as JP2006).
Modified 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.
Claims 1-2 and 6-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3 of U.S. Patent No. 9,061,003 B2 (the ‘003 patent) in view of Koizumi et al. (US 2016/0082087 A1, previously cited 10/2/2025), Lee et al. (Bioscience, Biotechnology, and Biochemistry, 83:6, 1146-1156) and JP2006151847A (referred as JP2006).
Claims 1 and 3 of the ‘003 patent disclosed a method and composition comprising a dipeptide and a tripeptide of Glu-Hyp-Gly.
Claims 1 and 3 of the ‘003 patent did not disclosed administration of a combination composition of comprising the peptide sequences of Gly-Pro and Glu-Hyp-Gly.
The relevancy of Koizumi et al. in view of Lee et al. and JP2006151847A as applied to claims 1-2 and 6-9 not repeated here.
Because Koizumi et al. in view of Lee et al. and JP2006151847A teach beneficial combination of Gly-Pro and Glu-Hyp-Gly in a collagen peptide mixture for oral administration, one of ordinary skill in the art would have found it obvious to combine the peptide of Glu-Hyp-Gly taught by claims 1 and 3 of the ‘003 patent with Koizumi et al.
Thus, claims 1 and 3 of the ‘003 patent in view of Koizumi et al. is obvious to the instant claims 1-2 and 6-9.
Response to Arguments
Applicant's arguments filed 12/31/2025 have been fully considered but they are not persuasive because the arguments do not apply to the modified rejection based on Koizumi et al. (US 2016/0082087 A1) in view of Lee et al. (Bioscience, Biotechnology, and Biochemistry, 83:6, 1146-1156) and JP2006151847A (referred as JP2006).
Claims 1-2 and 6-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 3 of U.S. Patent No. 12,569,532 (the ‘532 patent, scheduled patent issue date on 3/10/2026) in view of Koizumi et al. (US 2016/0082087 A1, previously cited 10/2/2025), Lee et al. (Bioscience, Biotechnology, and Biochemistry, 83:6, 1146-1156), and JP2006151847A (referred as JP2006).
Claim 1 of the ‘532 patent disclosed a therapeutic peptide of Glu-Hyp-Gly.
Claim 3 of the ‘532 patent disclosed the peptide derived from collagen.
The relevancy of Koizumi et al. in view of Lee et al. and JP2006151847A as applied to claims 1-2 and 6-9 not repeated here.
Because Koizumi et al. in view of Lee et al. and JP2006151847A teach beneficial combination of Gly-Pro and Glu-Hyp-Gly in a collagen peptide mixture for oral administration, one of ordinary skill in the art would have found it obvious to combine the peptide of Glu-Hyp-Gly taught by claims 1 and 3 of the ‘532 patent with Koizumi et al.
Thus, claims 1 and 3 of the ‘532 patent in view of Koizumi et al. is obvious to the instant claims 1-2 and 6-9.
Response to Arguments
Applicant's arguments filed 12/31/2025 have been fully considered but they are not persuasive because the arguments do not apply to the modified rejection based on Koizumi et al. (US 2016/0082087 A1) in view of Lee et al. (Bioscience, Biotechnology, and Biochemistry, 83:6, 1146-1156) and JP2006151847A (referred as JP2006).
Conclusion
No claim is allowed.
Applicant's amendment necessitated the 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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/J.L/Examiner, Art Unit 1658
26-February-2026
/LI N KOMATSU/ Primary Examiner, Art Unit 1658