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 .
Response to Election/Restriction filed on January 26, 2026 is acknowledged.
Claims 1-12 are pending in this application.
Priority
4. Applicant claims foreign priority to EP 20020536.7 (11/17/2020). The certified copy has been received by the Office. The document is in English. Therefore, the foreign priority dates has been perfected. Thus, the priority date of instant application is 11/17/2020.
Restriction
5. Applicant’s election of Group 1 (claims 1-11) in the reply filed on January 26, 2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Applicant elected with traverse of species palmitoyl-LSVD-OH for species of a fully defined tetrapeptide and ALAMCAT tetrapeptide as the species of a fully defined additional peptide. Applicant argues that “the unity of invention standard was not applied to support the election of species requirement”. The traversal in regards to the species election was found persuasive. Species election is hereby withdrawn. The restriction requirement between group inventions was deemed to be proper and is made FINAL in this office action. Claim 12 is withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected invention, there being no allowable generic or linking claim.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 are examined on the merits in this office action.
Objections
6. The abstract is objected to for the following minor informality:
Applicant is reminded of the proper language and format for an abstract of the disclosure.
The abstract should be in narrative form and generally limited to a single paragraph on a separate sheet within the range of 50 to 150 words. It is important that the abstract not exceed 150 words in length since the space provided for the abstract on the computer tape used by the printer is limited. The form and legal phraseology often used in patent claims, such as "means" and "said," should be avoided. The abstract should describe the disclosure sufficiently to assist readers in deciding whether there is a need for consulting the full patent text for details.
The language should be clear and concise and should not repeat information given in the title. It should avoid using phrases which can be implied, such as, "The disclosure concerns," "The disclosure defined by this invention," "The disclosure describes," etc.
In the instant case, the abstract recites a legal phraseology “said” for example, at line 18 of the abstract. Applicant should correct these informalities. See MPEP 608.01(b).
7. The specification is objected to for containing referring to sequences without also identifying them by the sequence identifier assigned to them in the sequence listing as required by 37 CFR 1.821(d). The specification discloses peptide sequences, and these are missing their respective sequence identifiers. For example, paragraphs [0010], [0024], [0142], [0152], [0155] and so on of instant specification US 2023/0416304 A1 disclose peptide sequences, but these are missing their sequence identifiers. The examiner would like to bring the applicant’s attention to the following excerpt from MPEP §2422.03:
37 CFR 1.821(d) requires the use of the assigned sequence identifier in all instances where the description or claims of a patent application discuss sequences regardless of whether a given sequence is also embedded in the text of the description or claims of an application. This requirement is also intended to permit references, in both the description and claims, to sequences set forth in the "Sequence Listing" by the use of assigned sequence identifiers without repeating the sequence in the text of the description or claims. Sequence identifiers can also be used to discuss and/or claim parts or fragments of a properly presented sequence. For example, language such as "residues 14 to 243 of SEQ ID NO:23" is permissible and the fragment need not be separately presented in the "Sequence Listing." Where a sequence is embedded in the text of an application, it must be presented in a manner that complies with the requirements of the sequence rules.
The applicant is therefore required to amend the specification to comply with 37 CFR 1.821(d).
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.
8. Claim 1 is objected to for the following minor informality: Claim 1 recites, “…Z is selected from the group consisting of OH, O R1, NHR1 or NR1R2…” There appears to be a space in between “O” and “R1” in the recitation of “O R1”. Applicant is required to correct this error.
9. Claims 4-6 are objected to for the following reason: Claims 4-6 recite amino acid sequences, for example U-LSVD-Z (see claim 4). The peptide sequences are missing the sequence identifiers. The proper way to claim a peptide sequence is for example, U-LSVD-Z (SEQ ID NO: 1) (see 37 CFR 1.821(d)). These errors should be corrected.
10. Claims 2-8 and 10-11 are objected to for the following: claims 2-8 recite the preamble, “A tetrapeptide according to claim 1…” Since claims 2-8 depend from independent claim 1, these should be corrected to “The tetrapeptide according to claim 1…”. Claims 10-11 recite the preamble, “A cosmetic composition according to claim 9…” Since claims 10-11 depend from independent claim 9, these should be corrected to “The cosmetic composition according to claim 9…”
11. Claims 2-3 are objected to because of the following informalities. Claims 2-3 do not have the correct capitalization for the phrase “SEQ ID NO: X”. These phrases should not have a lower case “o” present. Appropriate corrections are required.
Rejections
U.S.C. 112(b)
12. 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.
13. Claims 1-11 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.
14. Claim 1 recites, “A tetrapeptide, capable of inducing dermal extracellular matrix…said groups comprising from 1 to 24 carbon atoms and being capable of including one or more heteroatoms O, S, and/or N.” 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”. Furthermore, it is unclear under what conditions 1 to 24 carbon atoms would be incapable of including heteroatoms. It is not clear what scientific principle is referred to by “being capable of including one or more heteroatoms O, S and/or N”. Because claims 2-11 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.
15. Claim 1 recites, “A tetrapeptide…having the amino acid sequence U-LSXX-Z wherein…X denotes an amino acid selected from the group consisting of Valine (V), Aspartic acid (D), Proline (P), Glycine (G) and mixtures thereof…” It is unclear how the “X” can be “mixtures thereof” since the claims are drawn to a tetrapeptide. The amino acid sequence U-LSXX-Z comprises 2 X variables. Thus, if each X is “mixtures thereof”, the peptide sequence would be more than 6 residues. Therefore, the metes and bounds of the claim is unclear. Because claims 7-11 depend from indefinite claim 1 and do not clarify the point of confusion, these claims are also rejected under 35 U.S.C. 112, second paragraph.
16. Claim 1 recites, “…U is selected from the group consisting of H, -CO-R1…biotinyl group…R2 are independently selected from the group consisting of…aryloxy group…said groups comprising from 1 to 24…” It is unclear what “group” the term “said groups” is referring to. This could refer back to U or Z or refer back to R1, R2, etc. Therefore, the metes and bound of the claim is unclear. Because claims 2-11 depend from indefinite claim 1 without clarifying the point of confusion, these claims are also rejected under 35 U.S.C. 112, second paragraph.
Improper Markush
17. Claims 2-3 are rejected on the judicially created basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F. 2d 716, 721-22 (CCPA 1980) and Ex parte Hazumi, 3 USPQ 2d 1059, 1060 (BPAI 1984). The improper Markush grouping includes species of the claimed invention that do not share both a substantial structural feature and a common use that flows from the substantial structural feature. The members of the improper Markush grouping do not share a substantial feature and/or a common use that flows from the substantial structural feature for the following reasons: For example, instant SEQ ID NOs: 1-3 have the core sequence LSV (LSVD, LSVP, and LSVG); instant SEQ ID NOs: 4-6 have the core sequence LSD (LSDV, LSDP, and LSVG); instant SEQ ID NOs: 7-9 have the core sequence LSP (LSPV, LSPD, LSPG); and instant SEQ ID NOs: 10-12 have the core sequence LSG (LSGV, LSGD and LSGP). Thus, instant SEQ ID NOs: 1-3 share a core sequence; instant SEQ ID NOs: 4-6 share a core sequence; instant SEQ ID NOs: 7-9 share a core sequence; and instant SEQ ID NOs: 10-12 share a core sequence.
In response to this rejection, Applicant should either amend the claim(s) to recite only individual species or grouping of species that share a substantial structural feature as well as a common use that flows from the substantial structural feature, or present a sufficient showing that the species recited in the alternative of the claims(s) share a substantial structural feature as well as a common use that flows from the substantial structural feature. This is a rejection on the merits and may be appealed to the Board of Patent Appeals and Interferences in accordance with 35 U.S.C. § 134 and 37 CFR 41.31 (a)(1) (emphasis provided).
U.S.C. 112(a)
18. 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.
19. Claims 1-11 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.
The courts have stated:
“To fulfill the written description requirement, a patent specification must describe an invention and do so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d at 1966.” Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the Application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient.” MPEP 2163.
Further, for a broad generic claim, the specification must provide adequate written description to identify the genus of the claim. In Regents of the University of California v. Eli Lilly & Co., the court stated:
“A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials. Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284-85 (CCPA 1973) ("In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus. . . ."). Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The MPEP further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the sequence, it is “not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence.” MPEP 2163. The MPEP does state that for generic claim the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. MPEP 2163. If the genus has a substantial variance, the disclosure must describe a sufficient variety of species to reflect the variation within that genus. See MPEP 2163. Although the MPEP does not define what constitute a sufficient number of representative, the Courts have indicated what do not constitute a representative number species to adequately describe a broad generic. In Gostelli, the Court determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus. In re Gostelli, 872 F.2d at 1012, 10 USPQ2d at 1618.
In the instant case, the claims are drawn to a tetrapeptide, capable of inducing dermal extracellular matrix protein upregulation, selected from the group consisting of tetrapeptides having the amino acid sequence U-LSXX-Z wherein…U is selected from the group consisting of H, -CO-R1, -SO2-R1 or biotinyl group, at the C-terminal end, Z is selected from the group consisting of OH, OR1, NHR1 or NR1R2…R1 and R2 are independently selected from the group consisting of alkyl, aryl, aralkyl, alkylaryl, alkoxy, saccharide and aryloxy group…said groups comprising from 1 to 24 carbon atoms and being capable of including one or more heteroatoms O, S and/or N, and a cosmetic composition comprising the same. The generic statements “R1 and R2 groups may have up to 24 carbon atoms in a multitude of arrangements, giving rise to an extremely large genus do not provide ample written description for the compounds since the claims do not describe a single structural feature. The specification does not clearly define or provide examples of what qualify as compounds of the claimed invention.
As stated earlier, the MPEP states that written description for a genus can be achieved by a representative number of species within a broad generic. It is unquestionable claim 1 is broad generics with respect all possible compounds encompassed by the claims. The possible structural variations are limitless to any class of up to 24 carbon atoms attached to multiple tetrapeptides. It must not be forgotten that the MPEP states that if a peptide is described only by a functional characteristic, without any disclosed correlation between function and structure of the sequence, it is “not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence.” MPEP 2163. Here, though the claims may recite some functional characteristics, the claims lack written description because there is no disclosure of a correlation between function and structure of the compounds beyond compounds disclosed in the examples in the specification.
In this case, 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, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, but 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 inventor was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 2406 (MPEP 2163 (II.A.3.a.ii.)).
According to MPEP 2163 (II.A.3.a.ii.), a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 17890, 1790 (Fed. Cir. 2014).
Even when several species are disclosed, these are not necessarily representative of the entire genus. AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 17890, 1790 (Fed. Cir. 2014) (“The ‘128 and ‘485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, as here, one must describe a sufficient variety of species to reflect the variation within the genus to provide a “representative number” of species. Since each genus recite in the instant claims is large, it would be very challenging to describe sufficient species to cover the structures of the entire genus.
Applicant discloses several working examples all of which feature palmitoyl as “U” and hydroxyl group as “Z” (see for example, paragraphs [0024]-[0026]). Consequently, since only a limited number of species of tetrapeptides with “U” and “Z” components, are disclosed within the claimed genus above, the instant claims fail the written description requirement. Given this unpredictability of skin penetration effects, the skilled artisan would not have been in possession of the substantial repertoire of “U” and “Z” species encompassed by the claimed invention; one of skill in the art would conclude that Applicant was not in possession of the structural attributes of a representative number of species possessed by the members of the genus of every tetrapeptide recited by claim 1. One of skill in the art would conclude that the specification fails to disclose a representative number of species to describe the claimed genera.
Description of palmitoyl for “U” and OH for “Z” is not sufficient to encompass numerous other components that belong to the same genus. There is not sufficient amount of examples provided to encompass the numerous characteristics of the whole genus claimed.
For example, Robinson et al (Int. J. Cosmet. Sci., 2005, June 2005, 27(3): 155-160, abstract used and enclosed herein). Robinson et al teach pal-KTTKS and improved delivery across skin relative to KTTKS (see abstract). However, Hadgraft et al (International Journal of Pharmaceutics, 1996, 141(1-2): 17-25) teach that Azone and N-0915, which are superficially similar to palmitoyl, but have opposite skin penetration effects (see pages 18 and 21, Figs. 1 and 5).
In regards to claims 7-8, claims 7-8 do reduce the genera size of “U”, but does not alter the size of “Z” genera. Therefore, the specification fails to disclose a representative number of species to describe the claimed genera.
The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate"). Accordingly, it is deemed that the specification fails to provide adequate written description for the genus of the claims and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
U.S.C. 103
20. 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.
21. 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.
22. 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.
23. 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.
24. Claim(s) 1-3, 6-9 and 11 is/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 herein) and Lintner reference (WO 2005/048968).
25. Karin et al teach the same tetrapeptide sequence of instant SEQ ID NO: 8 (se 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 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 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).
26. 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).
27. 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).
28. 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).
29. 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).
30. Claim(s) 1-4, 7-9 and 11 is/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).
31. 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).
32. 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).
33. 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).
34. 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).
35. 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).
36. Claim(s) 1-3, 5, 7-9 and 11 is/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).
37. 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).
38. 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).
39. 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).
40. 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).
41. 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).
DOUBLE PATENTING
42. 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.
43. Claims 1-11 are 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). 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.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
44. Instant claims are drawn to:
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754
566
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Greyscale
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264
588
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.
45. Copending claims are drawn to:
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media_image3.png
880
724
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428
716
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406
736
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62
708
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.
46. Because the scope of instant claims and copending 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. Additionally, Harris et al teach a tetrapeptide GPKG (see SEQ ID NO: 32). 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).
And since instant claim 11 and copending claim 15 allows for additional peptide, one of ordinary skill in the art would have a reasonable expectation that the peptides can be combined.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
CONCLUSION
No claim is allowed.
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/JULIE HA/Primary Examiner, Art Unit 1654
2/12/2026