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 .
Amendment after Non-final office action filed on May 19, 2026 is acknowledged.
New claims 14-17 have been added.
Claims 1-12 and 14-17 are pending in this application.
Applicant elected Group 1 (claims 1-11) in the reply filed on January 26, 2026. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election had been treated as an election without traverse (MPEP 818.01(a)). Applicant elected with traverse of species palmitoyl-LSVD-OH for the species of a fully defined tetrapeptide and ALAMCAT tetrapeptide as the species of a fully defined peptide. Applicant’s arguments were found persuasive and the election of species was withdrawn in the previous office action. The restriction requirement between group inventions was deemed to be proper and was made FINAL in the previous office action. Claim 12 remains withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected invention, there being no allowable generic or linking claim. Claims 1-11 and 14-17 are examined on the merits in this office action.
This application contains claim 12, drawn to an invention nonelected without traverse in the paper of 1/26/2026. A complete reply to the final rejection must include cancellation of nonelected claims or other appropriate action (37 CFR 1.144). See MPEP § 821.01.
Terminal Disclaimer
The terminal disclaimer filed on 5/19/2026 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of US Application No. 18/037447 has been reviewed and is accepted. The terminal disclaimer has been recorded.
Withdrawn Objections and Rejections
Objection to the abstract is hereby withdrawn in view of Applicant’s amendment to the abstract.
Objection to the specification is hereby withdrawn in view of Applicant’s amendment to the specification.
Objection to claim 1 is hereby withdrawn in view of Applicant’s amendment to the claim.
Objection to claims 4-6 is hereby withdrawn in view of Applicant’s amendment to the claims.
Objection to claims 2-8 and 10-11 is hereby withdrawn in view of Applicant’s amendment to the claims.
Objection to claims 2-3 is hereby withdrawn in view of Applicant’s amendment to the claims.
Rejection of claims 1-11 under 35 U.S.C. 112(b) is withdrawn in part. Claims 1-11 and 14-17 are rejected under 35 U.S.C. 112(b) as set forth below
Rejection of claims 2-3 on the judicially created basis that it contains an improper Markush grouping of alternatives is hereby withdrawn in view of Applicant’s persuasive arguments.
Rejection of claims 1-11 under 35 U.S.C. 112(a) is hereby withdrawn in view of Applicant’s amendment to the claims and in view of Applicant’s persuasive arguments.
Rejection of claims 1-11 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 and 10-17 of copending Application No. 18/037447 (reference application) in view of Harris et al (WO 2007/146269, filed with IDS) and Lintner (WO 2005/048968, cited in the previous office action) is hereby withdrawn in view of Applicant filing terminal disclaimer on May 19, 2026.
Please note, the specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification. MPEP § 608.01.
Maintained and Revised Rejections
35 U.S.C. 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-8 and 14-15 remain/are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. This rejection is maintained and revised in view of Applicant’s amendment to the claims.
19. Claim 1 recites, “…a tetrapeptide capable of inducing dermal extracellular matrix protein upregulation…” It is unclear what is encompassed with the word “capable of”. The phrase “capable of” is not an absolute phrase. Capable does not state what actually occurs. The specification does not fully define what is meant by “capable of”. Because claims 2-8 and 14-15 depend from indefinite claim 1 and do not clarify the point of confusion, they must also be rejected under 35 U.S.C. 112, second paragraph.
Response to Applicant’s Arguments
20. Applicant argues that, “…the phrase “capable of inducing dermal extracellular matrix protein upregulation” as recited in the preamble of claim 1 is not improper. This language describes an inherent property of the tetrapeptides defined in claim 1, not an undefined functional limitation. The structural limitations in the body of claim 1 fully define the claimed tetrapeptide…a person of ordinary skill in the art would understand that tetrapeptides meeting these structural limitations possess this capability, as the specification teaches and demonstrates that tetrapeptides as claimed act to upregulate the production of proteins of the dermal extracellular matrix (ECM)…”
21. Applicant’s arguments have been fully considered but are not found persuasive. The phrase “capable of” implies that the peptide being claimed may or may not be able to perform or have the function being recited. As indicated in the rejection above, the phrase “capable of” is not an absolute phrase. Capable does not state what actually occurs. The specification does not fully define what is meant by “capable of”. Therefore, the rejection is deemed to be proper and is maintained herein.
U.S.C. 103
22. 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.
23. 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.
24. 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.
25. 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.
26. Claim(s) 1-3, 6-9, 11 and 14-17 remain/are rejected under 35 U.S.C. 103 as being unpatentable over Karin et al (US Patent No. 6514745, filed with IDS) in view of Smith et al (US Patent No. 4966848, cited in the previous office action) or Peers et al (US Patent No. 5837218, cited in the previous office action) or Smith et al (US Patent No. 5223421, cited in the previous office action), Robinson et al (Int. J. Cosmet. Sci., June 2005, 27(3): 155-160, abstract used and enclosed in the previous office action) and Lintner reference (WO 2005/048968, cited in the previous office action). The rejection is maintained and revised to include the new claims 14-17.
27. Karin et al teach the same tetrapeptide sequence of instant SEQ ID NO: 8 (see SEQ ID NO: 16, LSPD), meeting the limitation of instant claims 1-3 and 6, in part. Since Karin et al teach the same tetrapeptide of instant SEQ ID NO: 8, this peptide would inherently have the same functionality and activity as instant SEQ ID NO: 8. The MPEP § 2112 states: “Once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the Examiner presents evidence or reasoning tending to show inherency, the burden shifts to the Applicant to show an unobvious difference ‘[t]he PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on inherency’ under 35 U.S.C. 102, on prima facie obviousness’ under 35 U.S.C. 103, jointly or alternatively, the burden of proof is the same...[footnote omitted].” The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (quoting In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977)).” Therefore, the tetrapeptide of Karin et al would inherently have the same activity of inducing dermal extracellular matrix protein upregulation.
With respect to the limitation in the preamble of claim 9, “A cosmetic composition comprising the tetrapeptide,” please note that MPEP 2111.02 II states “a preamble generally is not limiting when the claim body describes a structurally complete invention such that deletion of the preamble phrase does not affect the structure or steps of the claimed invention.” In the instant case, the preamble does not affect the structure of the tetrapeptide. The preamble in this case recites a statement of purpose of use, and therefore was not treated as a claim limitation.
The difference between the instant claims and the Karin reference is that the reference does not teach the “U” and “Z” of the N-terminus and C-terminus of the tetrapeptide, respectively, and additional peptide in the cosmetic composition (additional ALAMCAT tetrapeptide, the elected species).
28. However, Smith et al *US Patent ‘848) teach that “An acetyl moiety was discovered as the amino-terminal blocking group of viral coat protein in 1958 and of hormonal peptide in 1959. Since then, a large number of proteins in various organisms have been shown to possess acetylated amino-terminal residues. For example, mouse L-cells and Ehrich ascites cells have about 80% of their intracellular soluble proteins Na-acetylated [and in] lower eukaryotic organisms, about 50%. These data demonstrate that N-acetyl is a very important blocking group. It has been suggested that the biological function of this blocking group may be to protect against premature protein catabolism and protein proteolytic degradation.” (see column 1, lines 18-37). Additionally, Peers et al (US Patent ‘218) teach that, “N- and C-terminal modification of peptides is common practice in the art of preparation of peptides having greater stability, particularly for in vivo use. Such modifications include the action of protecting groups such as the protecting groups used conventionally in the art of organic synthesis. Suitable N-terminal protecting groups include, for example, lower alkanoyl groups of the formula R-C(O)- in which R is a linear or branched lower alkyl…A preferred group for protecting the N-terminal end of the present compounds is the acetyl group, CH3C(O)” (see column 3, lines 15-25). The reference further teaches that “suitable C-terminal protecting groups include groups which form ketones or amides at the carbon atom of the C-terminal carboxyl, or groups which form esters at the oxygen atom of the carboxyl. Ketone and ester-forming groups include alkyl groups, particularly branched or unbranched lower alkyl” (see column 3, lines 28-33). Smith et al (US Patent ‘421) teach that, “Na-acetylation is the most common chemical modification of the a-amino acid group at the amino termini of eukaryotic proteins” (see column 3, lines 62-64). Additionally, “the rate of protein turnover mediated by the ubiquitin-dependent degradation system depends on the presence of a free a-amino group at the amino terminus of model proteins and [indicates that] Na-acetylation may play a crucial role in impeding protein turnover. Thus, Na-acetylation plays important roles in regulating diverse protein functions” (see column 4, lines 21-40).
29. Additionally, Robinson et al teach that the palmitoyl at the N-terminal end of a peptide (e.g., Pal-KTTKS) had significant improvement vs placebo control (KTTKS, without the N-terminal Pal) in skin penetration (see abstract).
30. Furthermore, Lintner reference teaches that pharmaceutical, personal care and cosmetic compositions containing a tripeptide and a tetrapeptide are useful for treating visible signs of aging including wrinkles, stretch marks and dark circles (see abstract). Lintner reference teaches tetrapeptide comprising, for example, N-Palmitoyl-TKPR (SEQ ID NO: 1) and N-Palmitoyl-GQPR (SEQ ID NO: 3) (see p. 2, lines 12-14). Lintner reference teaches ALAMCAT-tetrapeptides (see, for example, pp. 3-6). Lintner reference teaches that “repeated topical application of some combinations of tetrapeptides (rigin-based tetrapeptides, ALAMCAT-tetrapeptides or mixtures thereof) with tripeptide (His-based tripeptides, GHK-tripeptides or mixtures thereof) can offer at least some of the advantages and qualities…the ability to improve the visible signs of aging in human skin…and other skin texture defects…some benefit in tissue regeneration” (see p. 4, lines 11-27).
31. Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of Karin et al, Smith et al or Peers et al or Smith et al, Robinson et al and Lintner reference to have Na-acetylated and C-termini ester modified peptides for the benefit of protecting the peptide from proteolytic degradation and premature protein catabolism, add the palmitoyl at the N-terminal ends to short peptides to benefit skin penetration and skin improvement (such as fine lines and wrinkle improvement), and add in additional tetrapeptides for skin improvement. One would have been motivated to acetylate the N-terminus and make an ester modification of the C-terminus, in order to mimic ‘the most common chemical modification’ of eukaryotic proteins, protect the peptide from proteolytic degradation and premature catabolism, as protecting the N- and C-terminus is 'common practice in the art' (see Peers, above) and acetyl group is 'a very important blocking group' (Smith, above), or to add in palmitoyl at the N0terminal ends to improve the skin penetration effect. One would have had a reasonable expectation of success in forming these N- and C-terminal modified peptides, because it is 'common practice in the art' (Peers, above) to modify the N-terminus with the most common chemical modification' of eukaryotic proteins (Smith, above), and is a technique practiced widely in the art (Peers and Smith, above).
32. Claim(s) 1-4, 7-9 and 11 and 14-17 remain/are rejected under 35 U.S.C. 103 as being unpatentable over Merten et al (US 2006/0099689) in view of Smith et al (US Patent No. 4966848, cited in the previous office action) or Peers et al (US Patent No. 5837218, cited in the previous office action) or Smith et al (US Patent No. 5223421, cited in the previous office action), Robinson et al (Int. J. Cosmet. Sci., June 2005, 27(3): 155-160, abstract used and enclosed herein) and Lintner reference (WO 2005/048968). The rejection is maintained and revised to include the new claims 14-17.
33. Merten et al teach same tetrapeptide sequence of instant SEQ ID NO: 1 (see SEQ ID NO: 52, LSPD), meeting the limitation of instant claims 1-4, in part. Since Merten et al teach the same tetrapeptide of instant SEQ ID NO: 1, this peptide would inherently have the same functionality and activity as instant SEQ ID NO: 1. The MPEP § 2112 states: “Once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the Examiner presents evidence or reasoning tending to show inherency, the burden shifts to the Applicant to show an unobvious difference ‘[t]he PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on inherency’ under 35 U.S.C. 102, on prima facie obviousness’ under 35 U.S.C. 103, jointly or alternatively, the burden of proof is the same...[footnote omitted].” The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (quoting In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977)).” Therefore, the tetrapeptide of Merten et al would inherently have the same activity of inducing dermal extracellular matrix protein upregulation.
With respect to the limitation in the preamble of claim 9, “A cosmetic composition comprising the tetrapeptide of claim,”, please note that MPEP 2111.02 II states "a preamble generally is not limiting when the claim body describes a structurally complete invention such that deletion of the preamble phrase does not affect the structure or steps of the claimed invention." In the instant case, the preamble does not affect the structure of the tetrapeptide. The preamble in this case recites a statement of purpose or use, and therefore was not treated as a claim limitation.
The difference between the instant claims and the Merten reference is that the reference does not teach the “U” and “Z” of the N-terminus and C-terminus of the tetrapeptide, respectively, and additional peptide in the cosmetic composition (additional ALAMCAT tetrapeptide, the elected species).
34. However, Smith et al (US Patent ‘848) teach that “An acetyl moiety was discovered as the amino-terminal blocking group of viral coat protein in 1958 and of hormonal peptide in 1959. Since then, a large number of proteins in various organisms have been shown to possess acetylated amino-terminal residues. For example, mouse L-cells and Ehrich ascites cells have about 80% of their intracellular soluble proteins Na-acetylated [and in] lower eukaryotic organisms, about 50%. These data demonstrate that N-acetyl is a very important blocking group. It has been suggested that the biological function of this blocking group may be to protect against premature protein catabolism and protein proteolytic degradation.” (see column 1, lines 18-37). Additionally, Peers et al (US Patent ‘218) teach that, “N- and C-terminal modification of peptides is common practice in the art of preparation of peptides having greater stability, particularly for in vivo use. Such modifications include the action of protecting groups such as the protecting groups used conventionally in the art of organic synthesis. Suitable N-terminal protecting groups include, for example, lower alkanoyl groups of the formula R-C(O)- in which R is a linear or branched lower alkyl…A preferred group for protecting the N-terminal end of the present compounds is the acetyl group, CH3C(O)” (see column 3, lines 15-25). The reference further teaches that “suitable C-terminal protecting groups include groups which form ketones or amides at the carbon atom of the C-terminal carboxyl, or groups which form esters at the oxygen atom of the carboxyl. Ketone and ester-forming groups include alkyl groups, particularly branched or unbranched lower alkyl” (see column 3, lines 28-33). Smith et al (US Patent ‘421) teach that, “Na-acetylation is the most common chemical modification of the a-amino acid group at the amino termini of eukaryotic proteins” (see column 3, lines 62-64). Additionally, “the rate of protein turnover mediated by the ubiquitin-dependent degradation system depends on the presence of a free a-amino group at the amino terminus of model proteins and [indicates that] Na-acetylation may play a crucial role in impeding protein turnover. Thus, Na-acetylation plays important roles in regulating diverse protein functions” (see column 4, lines 21-40).
35. Additionally, Robinson et al teach that the palmitoyl at the N-terminal end of a peptide (e.g., Pal-KTTKS) had significant improvement vs placebo control (KTTKS, without the N-terminal Pal) in skin penetration (see abstract).
36. Furthermore, Lintner reference teaches that pharmaceutical, personal care and cosmetic compositions containing a tripeptide and a tetrapeptide are useful for treating visible signs of aging including wrinkles, stretch marks and dark circles (see abstract). Lintner reference teaches tetrapeptide comprising, for example, N-Palmitoyl-TKPR (SEQ ID NO: 1) and N-Palmitoyl-GQPR (SEQ ID NO: 3) (see p. 2, lines 12-14). Lintner reference teaches ALAMCAT-tetrapeptides (see, for example, pp. 3-6). Lintner reference teaches that “repeated topical application of some combinations of tetrapeptides (rigin-based tetrapeptides, ALAMCAT-tetrapeptides or mixtures thereof) with tripeptide (His-based tripeptides, GHK-tripeptides or mixtures thereof) can offer at least some of the advantages and qualities…the ability to improve the visible signs of aging in human skin…and other skin texture defects…some benefit in tissue regeneration” (see p. 4, lines 11-27).
37. Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of Merten et al, Smith et al or Peers et al or Smith et al, Robinson et al and Lintner reference to have Na-acetylated and C-termini ester modified peptides for the benefit of protecting the peptide from proteolytic degradation and premature protein catabolism, add the palmitoyl at the N-terminal ends to short peptides to benefit skin penetration and skin improvement (such as fine lines and wrinkle improvement), and add in additional tetrapeptides for skin improvement. One would have been motivated to acetylate the N-terminus and make an ester modification of the C-terminus, in order to mimic ‘the most common chemical modification’ of eukaryotic proteins, protect the peptide from proteolytic degradation and premature catabolism, as protecting the N- and C-terminus is 'common practice in the art' (see Peers, above) and acetyl group is 'a very important blocking group' (Smith, above), or to add in palmitoyl at the N0terminal ends to improve the skin penetration effect. One would have had a reasonable expectation of success in forming these N- and C-terminal modified peptides, because it is 'common practice in the art' (Peers, above) to modify the N-terminus with the most common chemical modification' of eukaryotic proteins (Smith, above), and is a technique practiced widely in the art (Peers and Smith, above).
38. Claim(s) 1-3, 5, 7-9, 11 and 14-17 remain/are rejected under 35 U.S.C. 103 as being unpatentable over Tseng-Law et al (US Patent No. 5968753) in view of Smith et al (US Patent No. 4966848, cited in the previous office action) or Peers et al (US Patent No. 5837218, cited in the previous office action) or Smith et al (US Patent No. 5223421, cited in the previous office action), Robinson et al (Int. J. Cosmet. Sci., June 2005, 27(3): 155-160, abstract used and enclosed herein) and Lintner reference (WO 2005/048968). The rejection is maintained and revised to include the new claims 14-17.
39. Tseng-Law et al teach same tetrapeptide sequence of instant SEQ ID NO: 9 (see SEQ ID NO: 197, LSPG), meeting the limitation of instant claims 1-3 and 5, in part. Since Tseng-Law et al teach the same tetrapeptide of instant SEQ ID NO: 9, this peptide would inherently have the same functionality and activity as instant SEQ ID NO: 9. The MPEP § 2112 states: “Once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the Examiner presents evidence or reasoning tending to show inherency, the burden shifts to the Applicant to show an unobvious difference ‘[t]he PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on inherency’ under 35 U.S.C. 102, on prima facie obviousness’ under 35 U.S.C. 103, jointly or alternatively, the burden of proof is the same...[footnote omitted].” The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (quoting In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977)).” Therefore, the tetrapeptide of Tseng-Law et al would inherently have the same activity of inducing dermal extracellular matrix protein upregulation.
With respect to the limitation in the preamble of claim 9, “A cosmetic composition comprising the tetrapeptide of claim,”, please note that MPEP 2111.02 II states "a preamble generally is not limiting when the claim body describes a structurally complete invention such that deletion of the preamble phrase does not affect the structure or steps of the claimed invention." In the instant case, the preamble does not affect the structure of the tetrapeptide. The preamble in this case recites a statement of purpose or use, and therefore was not treated as a claim limitation.
The difference between the instant claims and the Tseng-Law reference is that the reference does not teach the “U” and “Z” of the N-terminus and C-terminus of the tetrapeptide, respectively, and additional peptide in the cosmetic composition (additional ALAMCAT tetrapeptide, the elected species).
40. However, Smith et al (US Patent ‘848) teach that “An acetyl moiety was discovered as the amino-terminal blocking group of viral coat protein in 1958 and of hormonal peptide in 1959. Since then, a large number of proteins in various organisms have been shown to possess acetylated amino-terminal residues. For example, mouse L-cells and Ehrich ascites cells have about 80% of their intracellular soluble proteins Na-acetylated [and in] lower eukaryotic organisms, about 50%. These data demonstrate that N-acetyl is a very important blocking group. It has been suggested that the biological function of this blocking group may be to protect against premature protein catabolism and protein proteolytic degradation.” (see column 1, lines 18-37). Additionally, Peers et al (US Patent ‘218) teach that, “N- and C-terminal modification of peptides is common practice in the art of preparation of peptides having greater stability, particularly for in vivo use. Such modifications include the action of protecting groups such as the protecting groups used conventionally in the art of organic synthesis. Suitable N-terminal protecting groups include, for example, lower alkanoyl groups of the formula R-C(O)- in which R is a linear or branched lower alkyl…A preferred group for protecting the N-terminal end of the present compounds is the acetyl group, CH3C(O)” (see column 3, lines 15-25). The reference further teaches that “suitable C-terminal protecting groups include groups which form ketones or amides at the carbon atom of the C-terminal carboxyl, or groups which form esters at the oxygen atom of the carboxyl. Ketone and ester-forming groups include alkyl groups, particularly branched or unbranched lower alkyl” (see column 3, lines 28-33). Smith et al (US Patent ‘421) teach that, “Na-acetylation is the most common chemical modification of the a-amino acid group at the amino termini of eukaryotic proteins” (see column 3, lines 62-64). Additionally, “the rate of protein turnover mediated by the ubiquitin-dependent degradation system depends on the presence of a free a-amino group at the amino terminus of model proteins and [indicates that] Na-acetylation may play a crucial role in impeding protein turnover. Thus, Na-acetylation plays important roles in regulating diverse protein functions” (see column 4, lines 21-40).
41. Additionally, Robinson et al teach that the palmitoyl at the N-terminal end of a peptide (e.g., Pal-KTTKS) had significant improvement vs placebo control (KTTKS, without the N-terminal Pal) in skin penetration (see abstract).
42. Furthermore, Lintner reference teaches that pharmaceutical, personal care and cosmetic compositions containing a tripeptide and a tetrapeptide are useful for treating visible signs of aging including wrinkles, stretch marks and dark circles (see abstract). Lintner reference teaches tetrapeptide comprising, for example, N-Palmitoyl-TKPR (SEQ ID NO: 1) and N-Palmitoyl-GQPR (SEQ ID NO: 3) (see p. 2, lines 12-14). Lintner reference teaches ALAMCAT-tetrapeptides (see, for example, pp. 3-6). Lintner reference teaches that “repeated topical application of some combinations of tetrapeptides (rigin-based tetrapeptides, ALAMCAT-tetrapeptides or mixtures thereof) with tripeptide (His-based tripeptides, GHK-tripeptides or mixtures thereof) can offer at least some of the advantages and qualities…the ability to improve the visible signs of aging in human skin…and other skin texture defects…some benefit in tissue regeneration” (see p. 4, lines 11-27).
43. Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of Tseng-Law et al, Smith et al or Peers et al or Smith et al, Robinson et al and Lintner reference to have Na-acetylated and C-termini ester modified peptides for the benefit of protecting the peptide from proteolytic degradation and premature protein catabolism, add the palmitoyl at the N-terminal ends to short peptides to benefit skin penetration and skin improvement (such as fine lines and wrinkle improvement), and add in additional tetrapeptides for skin improvement. One would have been motivated to acetylate the N-terminus and make an ester modification of the C-terminus, in order to mimic ‘the most common chemical modification’ of eukaryotic proteins, protect the peptide from proteolytic degradation and premature catabolism, as protecting the N- and C-terminus is 'common practice in the art' (see Peers, above) and acetyl group is 'a very important blocking group' (Smith, above), or to add in palmitoyl at the N0terminal ends to improve the skin penetration effect. One would have had a reasonable expectation of success in forming these N- and C-terminal modified peptides, because it is 'common practice in the art' (Peers, above) to modify the N-terminus with the most common chemical modification' of eukaryotic proteins (Smith, above), and is a technique practiced widely in the art (Peers and Smith, above).
Response to Applicant’s Arguments
44. Applicant argues that None of Karin, Merten, or Tseng-Law discloses or suggests isolated tetrapeptide compounds as claimed, let alone cosmetic applications comprising the same.” Applicant argues that “Karin relates generally to the field of protein kinases, oncogenes and oncoproteins…Karin’s SEQ ID NO: 16 (LSPD) is a “consensus sequence motif” with alternative residues (Leu/Ala at position 1, Asp/Glu at position 4), not a discrete, isolated tetrapeptide compound as claimed.” Applicant further argues that “Merten relates generally to the field of molecular biology, biotechnology or process engineering for the production of proteins or peptides. Merten’s SEQ ID NO: 52 (LSVD) is disclosed only as a caspase cleavage recognition site within the DCC (Deleted in Colorectal Cancer) protein—a 1447 amino acid transmembrane protein.” Applicant argues that “Tseng-Law relates to peptides used to mediate cell release from antibody binding, methods of isolating such peptides, and methods for the specific release of target cells captured by antibody selection from a heterogenous cell suspension. Tseng-Law’s SEQ ID NO: 197 (LSPG) is disclosed only as amino acids 107-110 within the CD34 antigen protein, identified as a potential epitope region for antibody binding.”
45. Applicant’s arguments have been fully considered but are not found persuasive. Instant claims are drawn to product claims, i.e., a tetrapeptide having the amino acid sequence U-LSXX-Z. Karin, Merten, and Tseng-Law references teach the tetrapeptide LSPD, LSVD and LSPG, respectively. Therefore, the tetrapeptides would inherently have ALL of the functions and activities as instant tetrapeptides LSPD, LSVD and LSPG. The MPEP § 2112 states: “Once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the Examiner presents evidence or reasoning tending to show inherency, the burden shifts to the Applicant to show an unobvious difference ‘[t]he PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on inherency’ under 35 U.S.C. 102, on prima facie obviousness’ under 35 U.S.C. 103, jointly or alternatively, the burden of proof is the same...[footnote omitted].” The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (quoting In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977)).” Additionally, the MPEP 2112.01 II states that “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. (Applicant argued that the claimed composition was a pressure sensitive adhesive containing a tacky polymer while the product of the reference was hard and abrasion resistant. “The Board correctly found that the virtual identity of monomers and procedures sufficed to support a prima facie case of unpatentability of Spada’s polymer latexes for lack of novelty.”) Since the Karin, Merten, and Tseng-Law references teach the tetrapeptide LSPD, LSVD and LSPG, respectively, and a chemical composition and its properties are inseparable, the tetrapeptides of Karin, Merten and Tseng-Law references must have ALL of the functionalities and activities of instant tetrapeptides. Therefore, the combined arts is prima facie obvious over instant claims. Thus, the rejections are deemed to be proper and are maintained herein.
New Rejection
U.S.C. 112(b)
46. The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
47. Claims 9-11 and 16-17 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
48. Claim 9 recites, “…a tetrapeptide capable of inducing dermal extracellular matrix protein upregulation…” It is unclear what is encompassed with the word “capable of”. The phrase “capable of” is not an absolute phrase. Capable does not state what actually occurs. The specification does not fully define what is meant by “capable of”. Because claims 10-11 and 16-17 depend from indefinite claim 9 and do not clarify the point of confusion, they must also be rejected under 35 U.S.C. 112, second paragraph.
DOUBLE PATENTING
49. 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.
50. Claims 9 and 16-17 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 11of copending Application No. 18/686955 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because if one of ordinary skill in the art practiced the claimed invention of instant claims, one would necessarily achieve the claimed invention of copending claims, and vice versa.
51. Instant claims are drawn to:
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388
690
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52. Copending claims are drawn to:.
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758
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126
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53. Instant claims and copending claims share the tetrapeptide having the amino acid sequence U-LSXX-Z. Instant claims and copending claims also recite “A cosmetic composition comprising”. Therefore, the scope of the claims are similar. If one of ordinary skill in the art practiced the claimed invention of instant claims, one would necessarily achieve the claimed invention of copending claims, and vice versa.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JULIE HA whose telephone number is (571)272-5982. The examiner can normally be reached Monday-Thursday 5:00 am- 6:30 pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LIANKO GARYU can be reached at 571-270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/JULIE HA/Primary Examiner, Art Unit 1654
6/17/2026
Prosecution Insights