DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
This application filed 04/25/2024 is a National Stage entry of PCT/CN2023/130633 , International Filing Date: 11/09/2023 claims foreign priority to 202211539374.1, filed 12/02/2022.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 05/07/2025 complies with the
provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the
examiner.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
The specification filed on 06/17/2024 does not recite appropriate sequence identifiers in the form of SEQ ID numbers. For example, please see: [0033], [0076]. The sequences recited in the specification must include SEQ ID numbers to properly identify the sequences. Appropriate correction is required.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Drawings
Figure 1 and 2 should be designated by a legend such as --Prior Art-- because only that which is old is illustrated. See MPEP § 608.02(g). Corrected drawings in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. The replacement sheet(s) should be labeled “Replacement Sheet” in the page header (as per 37 CFR 1.84(c)) so as not to obstruct any portion of the drawing figures. If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Objections
Claim 16 is objected to because of the following informalities: In line 15, Examiner respectfully requests Applicant to italicize the scientific name Dendrobium officinale. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Regarding claim 16, the phrase "preferably" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d). In the present instance, the claim recites the broad recitation ‘moisturizer’ and the claim also recited ‘preferably…amino acid moisturizing agent’ which is the narrower statement of the range/limitation.
Claim 16 contains the trademark/trade name SymSave®H. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe preservative and, accordingly, the identification/description is indefinite.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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.
Claim(s) 1, 3-17, 19 are rejected under 35 U.S.C. 103 as being unpatentable over Yang He, hereinafter He (CN113549139A; published 2021-07-26; machine translation Google patents; citations herein from the machine translation) in view of J. R. McArthur et al., hereinafter McArthur (J. R. McArthur et al., Orientation of µ-Conotoxin PIIIA in a Sodium Channel Vestibule, Based on Voltage Dependence of Its Binding, Mol Pharmacol 80:219–227, 2011).
Regarding claim 1, He teaches conus polypeptide, N-Asn-Gly-Ile-Cys-Cys-Gly-Phe-Pro-Arg-Ser-Cys-Gly-Ser-Arg-Asn-Cys-Lys-Pro-His-Arg-Cys-Cys-C, SEQ ID NO: 1 in He (see Disclosure of the invention, 5th paragraph) . The sequence in He, differs from the instant SEQ ID NO: 1 at the residues emphasized in the above-mentioned sequence, at residues 2, 12 and 17. SEQ ID NO: 1 in the instant claim is NAICCGFPRSCASRNCRPHRCC.
He does not teach that the residue at position 2 is Alanine; residue at position 12 is Alanine and residue at position 17 is Arginine.
McArthur teaches that conotoxin derivatives with charge-conserving mutations (R12K, R14K and K17R) show “apparent valence” values similar to those of wild type. Examiner notes that the K17R generates ‘R’ at position 17, identical to the instant SEQ ID NO: 1 (see Abstract). McArthur teaches that two mutations, R2A and G6K, yielded no significant change in “apparent valence”, i.e. Alanine at position 2 (see Abstract). McArthur teaches that at position Arg12, when the arginine is replaced by an alanine or a glutamine, the “apparent valence” is decreased to 0.21 ± 0.01 (3) or 0.27 ± 0.01 (3), respectively (see page 222, 4th paragraph).
Obviousness can be established by combining or modifying the teachings of the prior art to
produce the claimed invention where there is some teaching, suggestion, or motivation to do so. In re
Kahn, 441 F.3d 977, 986, 78 USPQ2d 1329, 1335 (Fed. Cir. 2006) (discussing rationale underlying the
motivation-suggestion-teaching test as a guard against using hindsight in an obviousness analysis).
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the conus polypeptide of He, by substituting residues suggested in McArthur to generate SEQ ID NO: 1 in the instant application. One motivated to do so would have a reasonable expectation of success as McArthur specifically teaches that charge-conserving mutations (R12K, R14K and K17R) show “apparent valence” values similar to those of wild type (see Abstract), that Arg12, S13D, and Arg20 exert a weaker influence (see page 226, 1st paragraph, last few lines) and when position 2 is neutralized to alanine, the “apparent valence” values are not significantly different from that of the native toxin (see page 222, last paragraph). Thus, one would have recognized that applying the teaching in He to the method of McArthur, would have yielded predictable results, by substituting residues specifically suggested in McArthur, as McArther teaches that charges in certain positions do not contribute to PIIIA voltage dependence (See MPEP § 2143 l(A)(D)).
Regarding claim 3, the obviousness rationale has been set forth above in the teachings of He and McArthur. The claim limitation ‘wherein the …2,496.92 Da’, is directed to the sequence, derived from the combined teachings in He and McArthur, that is identical to the sequence as instantly claimed. Therefore, the claimed properties or functions are presumed to be inherent. Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). (See MPEP § 2112.01 (I)).
Regarding claim 4, in addition to the obviousness rationale stated above, He teaches preparation method which comprises the following steps: the conus polypeptide synthesized by adopting a solid-phase synthesis method or a prokaryotic recombinant expression method (see Disclosure of invention, 31st paragraph).
Regarding claim 5, He teaches crude conus polypeptide is synthesized and then the crude polypeptide is subjected to renaturation folding of a high-level structure (see Disclosure of invention, 32nd paragraph).
Regarding claim 6, He teaches renaturation by a glutathione redox method (see Disclosure of invention, 33rd paragraph).
Regarding claim 7, He teaches purifying the renatured and folded polypeptide (see Disclosure of invention, 34th paragraph).
Regarding claim 8, He teaches desalting purification by HPLC reverse phase column chromatography (see Disclosure of invention, 35th paragraph).
Regarding claim 9, He teaches that the conus polypeptide is synthesized by adopting a prokaryotic recombinant expression method, a prokaryotic expression plasmid needs to be constructed firstly, and then is expressed in Escherichia coli, and then is subjected to subsequent separation and purification (see Disclosure of invention, 36th paragraph). Regarding the claim limitation, wherein the prokaryotic…polypeptide, He teaches expression plasmid (see Disclosure of invention, 36th paragraph).
Regarding claim 10, embodiments of the specification disclose smoothing product as ‘modified cone snail polypeptide or the cone snail polypeptide obtained by the preparation method described as above in the preparation of an anti-wrinkle and/or wrinkle-smoothing product’ [0015]. He teaches the preparation of the modified cone snail polypeptide as noted in the rejection for claims 4-9. Examiner notes that embodiments of the specification do not disclose a wrinkle-smoothing product that is separate from the modified cone snail polypeptide.
Regarding claim 11, embodiments of the specification disclose ‘modified cone snail polypeptide or the cone snail polypeptide obtained by the preparation method described as above in the preparation of a sodium ion channel inhibition product’ [0044]. Examiner notes that embodiments of the specification do not disclose a sodium ion channel inhibition product that is separate from the modified cone snail polypeptide.
Regarding claim 12, He teaches a cosmetic preparation (see Technical Field).
Regarding claim 13, He teaches skeletal muscle sodium channel (see Detailed description, 3rd paragraph), cardiac muscle sodium channel (see Background, 3rd paragraph).
Regarding claim 14, He teaches wrinkle-removing product (see Background, 1st paragraph).
Regarding claim 15, He teaches cosmetic auxiliary materials and other cosmetic raw materials (see Disclosure of the invention, 17th paragraph). Specifically, He teaches humectant, emulsifier, mineral oil, vegetable oil, thickener, pH regulator and antiseptic (i.e. preservative) (see Disclosure of the invention, 19th paragraph). He teaches that cosmetic raw materials are selected from at least one of the following substances: polypeptide substances, plant extracts, cytokines and vitamins (see Disclosure of the invention, 25th paragraph).
Regarding claim 16, He teaches glycerin, polyalcohol, sodium hyaluronate, ceramide, trehalose, polysorbate-30 and an amino acid humectant. The glycerin may be used as a moisturizing agent or an antioxidant (see Disclosure of the invention, 20th paragraph); the emulsifier is selected from lanolin. In other embodiments, the emulsifier may be selected from polyglyceryl-10 stearate, octyl methicone, dimethicone, polymethylsilsesquioxane, babassu seed oil, phytosterol oleate, and the like (see Disclosure of the invention, 21st paragraph); thickening agent is selected from at least one of the following substances: carbomer, hydroxyethyl cellulose and xanthan gum. In other embodiments, the thickener may also be selected from hydroxyethyl acrylate/sodium acryloyldimethyl taurate copolymers (see Disclosure of the invention, 22nd paragraph); pH regulator is selected from at least one of the following substances: citric acid, sodium citrate, lactic acid, sodium lactate, triethanolamine, and arginine (see Disclosure of the invention, 23rd paragraph); preservative is selected from at least one of the following substances: 1, 2-hexanediol, p-hydroxyacetophenone (menthone), and ethylhexyl glycerol (see Disclosure of the invention, 24th paragraph); the polypeptide substance is selected from at least one of the following substances: carnosine, pentapeptide-3, glutathione, anserine and snake meat peptide (see Disclosure of the invention, 26th paragraph); plant extract is selected from at least one of the following substances: oat kernel extract and dendrobium officinale extract (see Disclosure of the invention, 27th paragraph); vitamins are selected from at least one of the following substances: vitamin B3, vitamin C and vitamin E (see Disclosure of the invention, 28th paragraph).
Regarding claim 17, He teaches a cosmetic preparation (see Technical Field).
Regarding claim 19, the obviousness rational is applied in the rejection for claim 3.
Claim(s) 2, 18 are rejected under 35 U.S.C. 103 as being unpatentable over Yang He, hereinafter He (CN113549139A; published 2021-07-26, machine translation Google patents; citations herein from the machine translation) in view of J. R. McArthur et al., hereinafter McArthur (J. R. McArthur et al., Orientation of µ-Conotoxin PIIIA in a Sodium Channel Vestibule, Based on Voltage Dependence of Its Binding, Mol Pharmacol 80:219–227, 2011) further in view of Seok-Jun Mun et al., hereinafter Mun (Seok-Jun Mun et al., Pathogen-derived peptides in drug targeting and its therapeutic approach, Journal of Controlled Release 350 (2022) 716–733).
The teachings of He and McArthur have been set forth above. Additionally, regarding claim 2, He and McArthur do not teach peptide acetylation at the N-terminus.
Mun teaches that peptides must be modified to increase protease resistance and reduce degradation by serum and tissue peptidases and proteases at the in vitro level. These modifications entail chemical modifications and alterations in vitro by various methods, including modifying natural amino acids in different labile sites in peptides to non-natural amino acids, along with C-terminal amidation and N-terminal acetylation (see page 725, section 3.3).
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the conus polypeptide of He and McArthur, by N-terminal acetylation as suggested in Mun. One motivated to do so would have a reasonable expectation of success, as Mun specifically teaches peptide stability in peptide-based drugs. Thus, one would have recognized that applying the teachings in He and McArthur, to the method of Mun, would have yielded predictable results, as Mun teaches that N-terminal acetylation increases protease resistance of peptides and reduces their degradation by serum and tissue peptidases and proteases (See MPEP § 2143 l(A)(D)).
Regarding claim 18, the teachings in He, McArthur and Mun have been noted above.
Consequently, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the conus polypeptide of He and McArthur, by N-terminal acetylation as suggested in Mun, in a cosmetic product. One motivated to do so would have a reasonable expectation of success, as Mun specifically teaches peptide stability in peptide-based drugs. Thus, one would have recognized that applying the teachings in He and McArthur, to the method of Mun, would have yielded predictable results, as He specifically teaches cosmetic preparation (see Technical Field) and that, as suggested in Mun, N-terminal acetylation increases protease resistance of peptides and reduces their degradation by serum and tissue peptidases and proteases (See MPEP § 2143 l(A)(D)).
Conclusion
No claim is allowed.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ARCHANA VARADARAJ whose telephone number is (571)272-2366. The examiner can normally be reached Monday-Friday 10:00am-5:00pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa Fisher can be reached at 5712707430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ARCHANA VARADARAJ/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
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