The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s election of Group II, claims 2-5, in the reply filed on June 30, 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)).
Claims 1, 6-26 are withdrawn. Claims 2-5 are under consideration.
Priority: This application is a 371 of PCT/CN2021/108680, filed July 27, 2021, which claims benefit to provisional application 63/057933, filed July 29, 2020.
Failure to Comply with Sequence Rules
Where the description of a patent application discusses a sequence of 4 or more amino acids or a sequence of 10 or more nucleic acids, reference must be made to the sequence by use of the sequence identifier preceded by “SEQ ID NO:” in the text of the description even if the sequence is also embedded in the text of the description of the patent application (see 37 CFR 1.821, especially paragraphs (a)-(d)). The sequence identifier may be used in either the drawing or the Brief Description of Drawings (see MPEP 2422).
Objection to the Drawings
The drawings are objected to because at least Figs. 1, 2, 25B, 34B, recite a sequence without a corresponding SEQ ID NO. The sequences must be in computer readable form (CRF) for search. See MPEP 2422 for sequence compliance requirements. Appropriate correction is
required.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). 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 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.
Claims 2-3 are rejected under 35 U.S.C. 103 as being unpatentable over Li et al. (WO 2019101195; IDS 06.14.23) in view of Thorson et al. (1991 Methods in Molecular Biology Vol. 77: 43-73). Li et al. disclose providing functionalized peptides and peptide inhibitors that target or inhibit π-π-π stacking interactions in the YEATS domain (at least abstract, p. 1-4, example 1-2). Li et al. disclose generating inhibitors and that two inhibitors carrying a 2-furancarbonyl side chain (XL-07; alternate name: 4.7; Table 1) and a 5-oxazolecarbonyl side chain (XL-13; alternate name: 4.13; Table 1) resulted in the strongest inhibitory activities (at least p. 102). Li et al. disclose inhibitor XL-07 is a peptide comprising 2-furancarbonyl lysine (at least Table 2, Table 5). Li et al. disclose various peptide inhibitors comprising 2-furancarbonyl lysine (at least Table 2, Table 5). Li et al. disclose “peptide” as used herein includes oligomers of amino acids and small and large peptides, including polypeptides (at least p. 33). Li et al. disclose working examples of peptide synthesis incorporating 2-furancarbonyl lysine (at least p. 94-95) but do not explicitly teach translation of an RNA encoding said polypeptide. However, Li et al. disclose that the amino acid analogs are incorporated into the disclosed peptides; these amino acids can readily be incorporated into polypeptide chains by chemical synthesis or by charging tRNA molecules with the amino acid of choice and engineering genetic constructs that utilize, for example, amber codons, to insert the analog amino acid into a peptide chain in a site specific way (citing Thorson et al.) (p. 37-38).
Thorson et al. disclose recently, a biosynthetic approach has been developed that allows site-specific incorporation of unnatural amino acids into proteins; this method involves replacement of the codon for the amino acid of interest with the amber nonsense codon by conventional oligonucleotide-directed mutagenesis; a synthetic amber suppressor tRNA is then chemically aminoacylated with the desired unnatural amino acid and added to an in vitro transcription-translation system programmed with the mutagenized DNA (at least p. 43-44, also Fig. 1).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to arrive at the claimed method for making a polypeptide comprising a 2-furancarbonyl lysine, comprising translating an RNA encoding said polypeptide, where the RNA comprises an amber codon, and wherein the translating is carried out in the presence of tRNA charged with 2-furancarbonyl lysine and the translating stops at the amber codon (instant claim 2). The motivation to do so is given by the prior art Li et al., which disclose creating peptide inhibitors comprising 2-furancarbonyl lysine by charging tRNA molecules with the amino acid of choice and engineering genetic constructs that utilize, for example, amber codons, to insert the analog amino acid into a peptide chain in a site specific way. One of ordinary skill would have a reasonable expectation of success because methods for incorporating unnatural amino acids into polypeptides by charging tRNA molecules with the unnatural amino acid of interest in an in vitro transcription-translation system are known and practiced in the prior art.
Regarding instant claim 3, Li et al. disclose the unnatural amino acid to be incorporated by charged tRNA molecules is 2-furancarbonyl lysine (at least p. 37-38, 94-95, 102) and Thorson et al. disclose incorporating the unnatural amino acid in a protein in the presence of the charged tRNA molecule, the unnatural amino acid, and tRNA synthetase (at least p. 44, 45-61).
Claims 2-3, 4-5 are rejected under 35 U.S.C. 103 as being unpatentable over Li et al. (WO 2019101195; IDS 06.14.23) in view of Thorson et al. (1991 Methods in Molecular Biology Vol. 77: 43-73) and Wan et al. (2014 Biochimica et Biophysica Acta 1844: 1059-1070; IDS 06.14.23). The teachings of Li et al. in view of Thorson et al. over at least instant claims 2-3 are noted above.
Regarding instant claim 4, Wan et al. disclose that unlike most aminoacyl-tRNA synthetases pyrrolysyl-tRNA-synthetase (PylRS) displays high substrate side chain promiscuity, low selectivity towards its substrate α-amine, and low selectivity toward the anticodon of tRNAPyl (at least p. 1059). Wan et al. disclose these unique but ordinary features of PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of more than 100 non-canonical amino acids (at least p. 1059). Wan et al. disclose to date, more than 30 lysine derivatives have been genetically incorporated into proteins at amber codon in living cells using engineered PylRS-tRNAPyl pairs (at least p. 1065). Wan et al. disclose known PylRS mutants include a M. barkeri PylRS having the mutations L274A/C313F/Y349F (at least p. 1065, Table 1). Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the M. barkeri PylRS mutant L274A/C313F/Y349F of Wan et al. for the tRNA synthetase of Thorson et al. in the method for making a polypeptide comprising a 2-furancarbonyl lysine of Li et al. in view of Thorson et al. noted above. The motivation to do so is given by Wan et al., which disclose PylRS has unique features over aminoacyl-tRNA synthetases incorporating unnatural amino acids into proteins. One of ordinary skill would have a reasonable expectation of success because the prior art discloses PylRS as an aminoacyl-tRNA synthetase allow the Pyl incorporation machinery to be easily engineered for the genetic incorporation of Lys derivatives.
Regarding instant claim 5, Thorson et al. disclose the charged tRNA comprises CUA (at least p. 58, 60-61) and Wan et al. disclose the tRNAPyl comprises CUA (at least p. 1060, 1067). Therefore, it would be obvious to one of ordinary skill that the M. barkeri PylRS of Wan et al. pairs with a M. barkeri -tRNAPyl comprising CUA that is charged with 2-furancarbonyl lysine in the method for making a polypeptide comprising a 2-furancarbonyl lysine of Li et al. in view of Thorson et al. noted above.
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Marsha Tsay whose telephone number is (571)272-2938. The examiner can normally be reached M-F.
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, Manjunath N. Rao can be reached at 571-272-0939. 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.
/Marsha Tsay/Primary Examiner, Art Unit 1656
Prosecution Insights