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
Applicant’s election without traverse of Group I, claims 1-10, in the reply filed on December 23, 2025, is acknowledged.
Claims 11-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Applicant’s election without traverse of the octapeptide species SEQ ID NO: 5 in the reply filed on December 23, 2025, is acknowledged. The elected species SEQ ID NO: 5 has been searched and is not allowable. Therefore, the search has not been extended in accordance with MPEP § 803.02.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date under 35 U.S.C. 119(e) as follows:
The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of 35 U.S.C. 112(a) or the first paragraph of pre-AIA 35 U.S.C. 112, except for the best mode requirement. See Transco Products, Inc. v. Performance Contracting, Inc., 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994).
The disclosure of the prior-filed application, Application No. 63/089,424, fails to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, first paragraph for one or more claims of this application. The prior filed application fails to disclose octapeptides of SEQ ID NOs: 1-8.
The disclosure of the prior-filed application, Application Nos. 63/089,424, 63/218,068 and PCT/US21/54010, fail to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, first paragraph for one or more claims of this application. The prior filed applications fail to support the claims for the reasons presented in the written description and enablement rejections presented below.
The earliest effective filing date of claims 1-10 is April 7, 2023.
Claim Interpretation
The specification does not provide a limiting definition of the term “hexapeptide-11”. The NCBI Pubchem database states that Hexapeptide-11 is FVAPFP,1 which corresponds to instant SEQ ID NO: 19 and is also known as CAS RN 161258-30-6. The claim term “hexapeptide-11” is interpreted as FVAPFP (SEQ ID NO: 19).
The claim term “tetradecyl-diaminobutyroylvalyldiaminobutyric urea trifluoroacetate” has the following structure:
PNG
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780
1262
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Greyscale
and is also known as CAS RN 934368-60-2.2
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-10 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
BRI of claim 1 is a composition suitable for topical administration comprising an octapeptide and a hexapeptide, and having the function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. The octapeptide consists of an amino acid sequence that is eight amino acids in length, wherein each position may be any natural or nonnatural amino acid. The hexapeptide consists of an amino acid sequence that is six amino acids in length, wherein each position may be any natural or nonnatural amino acid. Even limited to the 20 naturally-occurring amino acids, the claims encompass an enormous number of combinations of octapeptide and hexapeptide: 208 octapeptides x 206 hexapeptides = 1.64 x 1018 combinations of octapeptide and hexapeptides. The scope of the octapeptide-hexapeptide combination is unchanged in dependent claims 2-3, 5, and 7-10. In dependent claim 4, the scope of the octapeptide is eight and the scope of the hexapeptide is 206 resulting in 8 octapeptides x 206 hexapeptides = 1.68 x 1013 combinations of octapeptide and hexapeptides. In dependent claim 6, the scope of the octapeptide is 208 and the scope of the hexapeptide is 1 resulting in 208 octapeptide x 1 hexapeptide = 2.56 x 1010 combinations of octapeptide and hexapeptides.
Only those sequences meeting the structural and functional requirements of the genus are encompassed by the claim. Therefore, the claim encompasses all of the sequences meeting the structural requirements that are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. Although with the aid of a computer it may be possible to determine the amino acid sequences of the peptides that meet the structural requirements of the claim (i.e. octapeptide and hexapeptides of any amino acid sequence), it is not readily apparent from the claims or the specification which of these sequences are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression.
The specification includes a very limited reduction to practice. In Example 1, hexapeptide-12, hexapeptide-11, and an octapeptide of unknown sequence were tested for their effect on hyaluronic acid synthase 2 (HAS2) and hyaluronidase 2 (HYAL2) expression. The test octapeptide stimulated HAS2 (Figure 1). Hexapeptide-11 upregulated HAS2 (Figure 2) and downregulated HYAL2 (Figure 3). In Example 2, an octapeptide of unknown sequence were tested for its effect on secretion of high molecular weight hyaluronic acid from dermal fibroblasts and keratinocytes, and on HA synthesis. The test octapeptide increased hyaluronic acid secretion and synthesis (Figures 4-8). In Example 3, hexapeptide-11 was tested for its effect on EGR3 expression. Hexapeptide-11 upregulated EGR3 (Figure 9). Examples 4-6 do not include any results or data.
As discussed above the claim scope is potentially enormous depending on how many of the sequences that meet the structural requirements are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. In comparison, the scope of the description which only includes one octapeptide species of unknown sequence and one hexapeptide species with relevant activity (hexapeptide-11), is extremely narrow. Therefore, one of ordinary skill in the art would not consider the reduction to practice to be representative of the full scope of the claimed genus. The instant specification has failed to meet the written description requirement by actual reduction to practice of a representative number of species alone.
The specification does not disclose a partial structure of a protein that meets the structural requirements of the genus. Although one of ordinary skill in the art could determine if a given amino acid sequence meets the structural requirements of the genus, it would not be possible to determine from the sequence alone if the octapeptide or hexapeptide is able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. Unless all sequences having eight or six amino acids are able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression, this description alone does not constitute a partial structure for the genus.
The data presented in the specification raise more questions about the physical properties of the genus than they answer. The data do not suggest the physical basis for the claimed function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression and therefore do not describe which substitutions, deletions or additions could be made while preserving function. The specification does not describe any mechanism of action let alone the physical basis for the mechanism. Understanding the physical basis for function is critical to determining which of the sequences that meet the structural requirements of the genus also meet the functional requirements of the genus.
The specification does not describe a general correlation between structure and function for the claimed genus. The specification fails to include the amino acid sequence of the single octapeptide reduced to practice let alone the roles of these eight amino acids in function. In addition, the specification fails to describe a mechanism of action for the hexapeptide and the role of the six amino acids of hexapeptide-11 in its function. As a result, it is impossible to predict, based on the specification, how changing any position will affect the claimed function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression.
Solid state peptide synthesis and the cloning, recombinant expression and purification of proteins is well-known in the art. It is not disputed that one of ordinary skill in the art could isolate, albeit with route experimentation and optimization, an octapeptide or hexapeptide of a given sequence provided that the sequence is known. Where the specification fails to provide description is in the structure of the peptide to make. For all of the reasons presented above, one of ordinary skill in the art would not know which of the countless peptides that meet the structural requirements of the claims would also be able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. The specification does not make clear which peptides are in the genus and which are not because it does not describe the physical basis for the claimed activity, stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. In other words, the specification does not describe which peptides to make.
In addition, there is a high level of unpredictability and complexity associated with peptide structure and function. The prior art discloses numerous peptide sequences that are octapeptides and hexapeptides and their use in topical compositions for skin. See for example Pintea et al. (Peptides: Emerging Candidates for the Prevention and Treatment of Skin Senescence: A Review. Biomolecules. 2025 Jan 9;15(1):88), Tang et al. (Peptides in Cosmetics: From Pharmaceutical Breakthroughs to Skincare Innovations. Cosmetics 2025, 12(3), 107) and Errante et al. (Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front. Chem. 2020, 8, 572923). However, the octapeptides and hexapeptides reviewed in Pintea et al., Tang et al., and Errante et al. are not taught to possess the function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. Pintea et al. and Errante et al. teach that palmitoyl hexapeptide-12, which meets the structural requirements of the claims, has a different function of reducing the production of pro-inflammatory cytokines by keratinocytes and fibroblasts, such as interleukine-6 (IL-6) (Section 3.1.3 Pintea et al.; Figure 1 Errante et al.). Pintea et al. and Errante et al. teach that acetyl hexapeptide-3, which meets the structural requirements of the claims, has a different function of destabilizing the SNARE complex and inhibiting acetylcholine exocytosis (Section 3.3.1 Pintea et al.; Figure 1 Errante et al.). Pintea et al. teach that acetyl hexapeptide-8, which meets the structural requirements of the claims, has a different function of affecting collagen formation (Section 5.7). Tang et al. teach that hexapeptide-9, which meets the structural requirements of the claims, has a different function of stimulating fibroblasts to enhance collagen production (Section 4.1.1). Tang et al. teach that hexapeptide-2, which meets the structural requirements of the claims, has a different function of blocking the interaction between α-MSH and the MC1R on skin cells, and preventing melanin synthesis and its transfer to surrounding cells (Section 4.2). Pintea et al. and Errante et al. teach that acetyl octapeptide-1/3, which meets the structural requirements of the claims, has a different function of destabilizing the SNARE complex and inhibiting acetylcholine exocytosis (Table 1 Pintea et al.; Figure 1 Errante et al.). These reviews make it clear that a peptide length of six or eight alone cannot predict possession of the claimed function.
The prior art discloses a peptide capable of stimulating hyaluronic acid but it is not an octapeptide or hexapeptide. Tang et al. teach that tetradecyl aminobutyroylvalylamino butyric urea trifluoroacetate (aka Syn-Hycan), a tripeptide, can enhance skin hydration by promoting the synthesis of hyaluronic acid (Section 4.3). Florence et al. (US 2012/0288478 A1) teach a peptide of the general formula R1-(AA)n-X1-X2-X3-Pro-X4-X5-X7-(AA)P-R2 is activates the synthesis of proteins of the aquaporin family, promoting water transport between skin cells and ensuring proper hydration across skin layers (abstract). However, these peptides have different structure and function than the claimed peptides further confirming that a peptide length of six or eight alone cannot predict possession of the claimed function.
For these reasons, the skilled artisan would not reasonably conclude that the inventor(s), at the time the application was filed, had possession of the full scope of the claimed invention.
Claims 1-10 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
To comply with the enablement requirements of 35 U.S.C. §112, first paragraph, a specification must adequately teach how to make and how to use a claimed invention throughout its scope, without undue experimentation. Plant Genetic Systems N.V. v. DeKalb Genetics Corp., 315 F.3d 1335, 1339, 65 USPQ2d 1452, 1455 (Fed. Cir. 2003). There are a variety of factors which may be considered in determining whether a disclosure would require undue experimentation. These factors include: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims. In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
The Nature of the Invention
Claims 1-10 are drawn to topical compositions containing octapeptides and hexapeptides.
The breadth of the claims
BRI of claim 1 is a composition suitable for topical administration comprising an octapeptide and a hexapeptide, and having the function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. The octapeptide consists of an amino acid sequence that is eight amino acids in length, wherein each position may be any natural or nonnatural amino acid. The hexapeptide consists of an amino acid sequence that is six amino acids in length, wherein each position may be any natural or nonnatural amino acid. Even limited to the 20 naturally-occurring amino acids, the claims encompass an enormous number of combinations of octapeptide and hexapeptide: 208 octapeptides x 206 hexapeptides = 1.64 x 1018 combinations of octapeptide and hexapeptides. The scope of the octapeptide-hexapeptide combination is unchanged in dependent claims 2-3, 5, and 7-10. In dependent claim 4, the scope of the octapeptide is eight and the scope of the hexapeptide is 206 resulting in 8 octapeptides x 206 hexapeptides = 1.68 x 1013 combinations of octapeptide and hexapeptides. In dependent claim 6, the scope of the octapeptide is 208 and the scope of the hexapeptide is 1 resulting in 208 octapeptide x 1 hexapeptide = 2.56 x 1010 combinations of octapeptide and hexapeptides.
Only those sequences meeting the structural and functional requirements of the genus are encompassed by the claim. Therefore, the claim encompasses all of the sequences meeting the structural requirements that are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. Although with the aid of a computer it may be possible to determine the amino acid sequences of the peptides that meet the structural requirements of the claim (i.e. octapeptide and hexapeptides of any amino acid sequence), it is not readily apparent from the claims or the specification which of these sequences are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression.
The State of the Prior Art and its Predictability
In addition, there is a high level of unpredictability and complexity associated with peptide structure and function. The prior art discloses numerous peptide sequences that are octapeptides and hexapeptides and their use in topical compositions for skin. See for example Pintea et al. (Peptides: Emerging Candidates for the Prevention and Treatment of Skin Senescence: A Review. Biomolecules. 2025 Jan 9;15(1):88), Tang et al. (Peptides in Cosmetics: From Pharmaceutical Breakthroughs to Skincare Innovations. Cosmetics 2025, 12(3), 107) and Errante et al. (Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front. Chem. 2020, 8, 572923). However, the octapeptides and hexapeptides reviewed in Pintea et al., Tang et al., and Errante et al. are not taught to possess the function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. Pintea et al. and Errante et al. teach that palmitoyl hexapeptide-12, which meets the structural requirements of the claims, has a different function of reducing the production of pro-inflammatory cytokines by keratinocytes and fibroblasts, such as interleukine-6 (IL-6) (Section 3.1.3 Pintea et al.; Figure 1 Errante et al.). Pintea et al. and Errante et al. teach that acetyl hexapeptide-3, which meets the structural requirements of the claims, has a different function of destabilizing the SNARE complex and inhibiting acetylcholine exocytosis (Section 3.3.1 Pintea et al.; Figure 1 Errante et al.). Pintea et al. teach that acetyl hexapeptide-8, which meets the structural requirements of the claims, has a different function of affecting collagen formation (Section 5.7). Tang et al. teach that hexapeptide-9, which meets the structural requirements of the claims, has a different function of stimulating fibroblasts to enhance collagen production (Section 4.1.1). Tang et al. teach that hexapeptide-2, which meets the structural requirements of the claims, has a different function of blocking the interaction between α-MSH and the MC1R on skin cells, and preventing melanin synthesis and its transfer to surrounding cells (Section 4.2). Pintea et al. and Errante et al. teach that acetyl octapeptide-1/3, which meets the structural requirements of the claims, has a different function of destabilizing the SNARE complex and inhibiting acetylcholine exocytosis (Table 1 Pintea et al.; Figure 1 Errante et al.). These reviews make it clear that a peptide length of six or eight alone cannot predict possession of the claimed function.
The prior art discloses a peptide capable of stimulating hyaluronic acid but it is not an octapeptide or hexapeptide. Tang et al. teach that tetradecyl aminobutyroylvalylamino butyric urea trifluoroacetate (aka Syn-Hycan), a tripeptide, can enhance skin hydration by promoting the synthesis of hyaluronic acid (Section 4.3). Florence et al. (US 2012/0288478 A1) teach a peptide of the general formula R1-(AA)n-X1-X2-X3-Pro-X4-X5-X7-(AA)P-R2 is activates the synthesis of proteins of the aquaporin family, promoting water transport between skin cells and ensuring proper hydration across skin layers (abstract). However, these peptides have different structure and function than the claimed peptides further confirming that a peptide length of six or eight alone cannot predict possession of the claimed function.
The Level of Skill in the Art
Solid state peptide synthesis and the cloning, recombinant expression and purification of proteins is well-known in the art. It is not disputed that one of ordinary skill in the art could isolate, albeit with route experimentation and optimization, an octapeptide or hexapeptide of a given sequence provided that the sequence is known. Where the specification fails to provide description is in the structure of the peptide to make. For all of the reasons presented above, one of ordinary skill in the art would not know which of the countless peptides that meet the structural requirements of the claims would also be able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. The specification does not make clear which peptides are in the genus and which are not because it does not describe the physical basis for the claimed activity, stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression. In other words, the specification does not describe which peptides to make.
The Level of Guidance in the Specification
The data presented in the specification raise more questions about the physical properties of the genus than they answer. The data do not suggest the physical basis for the claimed function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression and therefore do not describe which substitutions, deletions or additions could be made while preserving function. The specification does not describe any mechanism of action let alone the physical basis for the mechanism. Understanding the physical basis for function is critical to determining which of the sequences that meet the structural requirements of the genus also meet the functional requirements of the genus.
The specification does not describe a general correlation between structure and function for the claimed genus. The specification fails to include the amino acid sequence of the single octapeptide reduced to practice let alone the roles of these eight amino acids in function. In addition, the specification fails to describe a mechanism of action for the hexapeptide and the role of the six amino acids of hexapeptide-11 in its function. As a result, it is impossible to predict, based on the specification, how changing any position will affect the claimed function of stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression.
The Presence or Absence of Working Examples
The specification includes a very limited reduction to practice. In Example 1, hexapeptide-12, hexapeptide-11, and an octapeptide of unknown sequence were tested for their effect on hyaluronic acid synthase 2 (HAS2) and hyaluronidase 2 (HYAL2) expression. The test octapeptide stimulated HAS2 (Figure 1). Hexapeptide-11 upregulated HAS2 (Figure 2) and downregulated HYAL2 (Figure 3). In Example 2, an octapeptide of unknown sequence were tested for its effect on secretion of high molecular weight hyaluronic acid from dermal fibroblasts and keratinocytes, and on HA synthesis. The test octapeptide increased hyaluronic acid secretion and synthesis (Figures 4-8). In Example 3, hexapeptide-11 was tested for its effect on EGR3 expression. Hexapeptide-11 upregulated EGR3 (Figure 9). Examples 4-6 do not include any results or data.
As discussed above the claim scope is potentially enormous depending on how many of the sequences that meet the structural requirements are also able to stimulate hyaluronic acid synthesis, increase HAS2 expression, reduce HYAL2 expression, or increase EGR3 expression. In comparison, the scope of the description which only includes one octapeptide species of unknown sequence and one hexapeptide species with relevant activity (hexapeptide-11), is extremely narrow. Therefore, one of ordinary skill in the art would not consider the reduction to practice to be representative of the full scope of the claimed genus.
The Quantity of Experimentation Necessary
Considering the factors above, the skilled artisan would be burdened with undue experimentation in determining if one of the claimed octapeptide-hexapeptide combinations would be effective at stimulating hyaluronic acid synthesis, increasing HAS2 expression, reducing HYAL2 expression, or increasing EGR3 expression . The skilled artisan would be burdened with testing a broad range of peptides in in vitro assays for each function. The active inhibitors would then have to be subjected to animal models for topical administration. The experimentation required represents years of inventive effort. When the above factors are weighed, it is the examiner's position that one skilled in the art could not practice the invention without undue experimentation.
Therefore, in view of the Wands factors, the claims appear to require undue experimentation to use the full scope of the claimed invention.
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, 4, and 6 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 19/064,198 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the reference claims anticipate and/or render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reference claim 18 recites a topical composition (aka a composition for administration to the skin) comprising an octapeptide consisting of instant SEQ ID NO: 5, a hexapeptide, and a pharmaceutically-acceptable carrier, satisfying all of the structural limitations of instant claims 1 and 4. The composition has the effect of promoting cellular production of hyaluronic acid, thereby satisfying the functional limitation of instant claims 1 and 4 “stimulates hyaluronic acid synthesis”. Therefore, reference claim 18 anticipates instant claims 1 and 4.
With respect to claim 2, reference claim 17 requires that the composition further comprises a tripeptide. It would have been obvious to combine the octapeptide-tripeptide composition of reference claim 17 with the octapeptide-hexapeptide of reference claim 18 because both were taught to be useful for the same purpose of promoting cellular production of hyaluronic acid (MPEP § 2144.06(I)).
With respect to claim 6, reference claim 8 requires that the hexapeptide is hexapeptide-11.
Claims 1-10 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/913,677 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the reference claims anticipate and/or render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reference claim 8 recites a topical composition comprising an octapeptide and a hexapeptide, satisfying all of the structural limitations of instant claim 1. Reference claim 17 states that the composition has the effect of stimulating hyaluronic acid synthesis, thereby satisfying the functional limitation of instant claim 1. Therefore, reference claim 8 anticipates instant claim 1.
With respect to claim 2, reference claim 6 requires that the composition further comprises a synthetic tripeptide. It would have been obvious to combine the octapeptide-tripeptide composition of reference claim 6 with the octapeptide-hexapeptide of reference claim 8 because both were taught to be useful for the same purpose of reducing skin inflammation (MPEP § 2144.06(I)).
With respect to claim 3, reference claim 7 requires that the synthetic tripeptide is tetradecyl aminobutyroylvalylaminobutyric urea trifluoroacetate.
With respect to claim 4, reference claim 2 requires that the octapeptide is at least one of GDGDGASA (SEQ ID NO: 1), GPMGPSGP (SEQ ID NO: 2), GLGPGARA (SEQ ID NO: 3), GPQGFQGP (SEQ ID NO: 4), GPHGVREA (SEQ ID NO: 5), GPMGPRGP (SEQ ID NO: 6), or GPGKNGDD (SEQ ID NO: 7).
With respect to claim 5, given that reference claim 12 allows for encapsulating the other components of the composition in a liposome, it would have been obvious to encapsulate the octapeptide in a liposome.
With respect to claim 6, reference claim 9 requires that the hexapeptide is hexapeptide-11.
With respect to claim 7, reference claim 12 states that the hexapeptide-11 may be encapsulated in a liposome.
With respect to claims 8-10, reference claim 12 requires that the composition further comprises lactoferrin, or phosphatidylserine, wherein the lactoferrin, or the phosphatidylserine is encapsulated in a liposome.
Claims 1-10 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of copending Application No. 18/913,581 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the reference claims anticipate and/or render obvious the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Reference claim 2 recites a topical composition comprising an octapeptide GPHGVREA (SEQ ID NO: 1, aka instant SEQ ID NO: 5), tripeptide-1 and hexapeptide-12, satisfying all of the structural limitations of instant claims 1, 2, and 4. Reference claim 1 states that the composition has the effect of stimulating hyaluronic acid synthesis, thereby satisfying the functional limitation of instant claim 1. Therefore, reference claim 2 anticipates instants claim 1, 2, and 4.
With respect to claim 2, reference claim 7 requires that the composition further comprises a synthetic tripeptide.
With respect to claim 3, reference claim 7 requires that the synthetic tripeptide is tetradecyl aminobutyroylvalylaminobutyric urea trifluoroacetate.
With respect to claim 5, given that reference claim 12 allows for encapsulating the other components of the composition in a liposome, it would have been obvious to encapsulate the octapeptide in a liposome.
With respect to claim 6, reference claim 8 requires that the composition further comprises hexapeptide-11.
With respect to claim 7, reference claim 12 states that the hexapeptide-11 may be encapsulated in a liposome.
With respect to claims 8-10, reference claim 12 requires that the composition further comprises lactoferrin, or phosphatidylserine, wherein the lactoferrin, or the phosphatidylserine is encapsulated in a liposome.
Conclusion
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/CHRISTINA BRADLEY/Primary Examiner, Art Unit 1654
1 National Center for Biotechnology Information. "PubChem Compound Summary for CID 24998056, Hexapeptide-11" PubChem, https://pubchem.ncbi.nlm.nih.gov/compound/Hexapeptide-11. Accessed 12 January, 2026.
2 National Center for Biotechnology Information. "PubChem Compound Summary for CID 137528195, Tetradecyl aminobutyroylvalylaminobutyric urea trifluoroacetate" PubChem, https://pubchem.ncbi.nlm.nih.gov/compound/137528195. Accessed 12 January, 2026.