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 .
Status of the Claims
Claims 75 – 91 are currently pending and are the subject of this Office Action. This is the first Office Action on the merits of the claims.
Drawings
The drawings are objected to because FIGs. 1A – 8D include text and symbols that are illegible and must be modified so that they are clear.
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.
Specification
The use of the term nanobody, which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
The disclosure is objected to because of the following informalities: LGGSGRNAQVRLE in paragraphs 0172, 0173, and 0174 should be labeled with (SEQ ID NO: 53).
Appropriate correction is required.
Claim Rejections - 35 USC § 102
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 the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 75 and 89 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by DUGAL-TESSIER (Dugal-Tessier J, et al. Antibody-oligonucleotide conjugates: a twist to antibody-drug conjugates. Journal of Clinical Medicine. 2021 Feb 18;10(4):838; see PTO-892: Notice of References Cited).
The present application is directed to a targeting conjugate comprising a targeting moiety, a therapeutic agent, and an oligonucleotide, wherein the therapeutic agent and/or the oligonucleotide can be released from the targeting conjugate via cleavage.
According to the present specification, “[i]n some embodiments, the therapeutic agent is MMAE or a derivative thereof” (paragraph 0014 of the pre-grant publication).
According to the present specification, “the oligonucleotide is selected from the group consisting of: a double stranded DNA, a single stranded DNA, a double stranded RNA, a single stranded RNA, an antisense RNA, a small interference RNA (siRNA), a microRNA (miRNA), a short hairpin RNA (shRNA), and a CpG (Cytosine-phosphodiester-Guanine) oligonucleotide” (paragraph 0015 of the pre-grant publication).
DUGAL-TESSIER summaries the key technological advancements in the preparation of antibody–oligonucleotide conjugates (AOCs) and the distinct advantages and disadvantages of AOCs as novel therapeutics. See abstract. Teaches that the AOC is a carrier for a cytotoxin like an Antibody-drug conjugates (ADC). See p. 9, last paragraph.
Regarding claim 75, DUGAL-TESSIER teaches an AOC containing a single-strand oligonucleotide with trastuzumab as the targeting antibody and MMAE as the cytotoxin. See p. 9, last paragraph and figure 12A and B on p. 10. DUGAL-TESSIER also teaches an AOC with an antibody targeting Her2-expressing cell lines and with cleavable MMAE oligonucleotide constructs. See p. 12, second paragraph.
Thus, DUGAL-TESSIER anticipates a targeting conjugate comprising a targeting moiety, a therapeutic agent, and an oligonucleotide, wherein the therapeutic agent and/or the oligonucleotide can be released from the targeting conjugate via cleavage of present claim 1.
Regarding claim 89, DUGAL-TESSIER teaches a method of making the AOC (see p. 2, 2. Conjugation of Oligonucleotides to Antibodies – p. 11, 2.5. Summary).
Claim 87 is rejected under 35 U.S.C. 102(a)(1) as being anticipated by AJINOMOTO (WO 2020/090979-A1; published 05/07/2020; see PTO-892).
According to the present specification, “the TBF non-covalently binds to the targeting moiety” (paragraph 0096 of the pre-grant publication).
AJINOMOTO is directed to a compound that comprises a substance with an affinity for an antibody, a cleavage site and a reactive group, or a salt of the compound. See abstract. AJINOMOTO teaches that in recent years, it has been reported that the pharmacokinetics, the drug release rate, and the effect are changed by changing the binding number and binding position of ADC drug. For these reasons, it is required to control the number and position of the drug to be conjugated in the next-generation ADC, which may be achieved with modification of the antibody. See p. 3, Description. AJINOMOTO teaches a technique that enables modification of an antibody. See p. 3, last sentence.
Regarding claim 87, AJINOMOTO teaches formula (III ′): A-B2 '(-F2) -L'-B1' (-F1) -R'-T (III ') where A is an affinity substance for the antibody, R' is a moiety generated by the reaction between the antibody and the reactive group, T is an antibody. L' is a cleavable linker that is a divalent group containing a cleavable moiety, B1 ′ and B2 ′ are the same or different and each is a trivalent group containing a moiety generated by a reaction between a functional substance and a bioorthogonal functional group, F1 and F2 are the same or different and are functional substances. See p. 17, [20].
AJINOMOTO teaches that the functional substance may be a drug for any disease, such as MMAE or may be an oligonucleotide. See 3-2. Functional substance (F), p. 45 – 46.
Furthermore, AJINOMOTO teaches the sequence of SEQ ID NO: 75 of present claim 87 with 100% identity. AJINOMOTO’s SEQ ID NO: 54 is identical to present SEQ ID NO: 75 of present claim 80. See Appendix.
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.
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.
Claims 76 – 79, 81, 88 and 90 are rejected under 35 U.S.C. 103 as being unpatentable over DUGAL-TESSIER as applied to claim 75 and 89 above, and further in view of WALSH (Walsh SJ , et al . Site-selective modification strategies in antibody-drug conjugates. Chem Soc Rev. 2021 Jan 21;50(2):1305-1353; see PTO-892).
The teachings of DUGAL-TESSIER are discussed above and fully incorporated here. According to present claim 76, the domain labeled “B” is a targeting moiety binding fragment (TBF). According to the present specification, “the term ‘targeting moiety binding fragment’ or ‘TBF’ refers to a fragment comprising a targeting moiety binding peptide (‘TBP’) that specifically binds to a targeting moiety. The TBF may further comprise a chemical reactive moiety that can be covalently linked to the targeting moiety. In some embodiments, the TBF comprises a small molecule linker comprising the chemical reactive moiety. In some embodiments, the TBF does not comprise a chemical reactive moiety that can be covalently linked to the targeting moiety, i.e., the TBF non-covalently binds to the targeting moiety. In some embodiments, the targeting moiety binding peptide is an antibody binding peptide (‘ABP’), which is a polypeptide that specifically binds to an antibody. Exemplary ABPs include, but are not limited to, an FcBP-1, an FcBP-2, an Fc-III and fragments thereof. As used herein, a TBF comprising an ABP is referred herein as an ‘antibody binding fragment’ or ‘ABF’ “ (paragraph 0096 of the pre-grant publication).
According to the present specification, “[s]uitable cleavable linkers include, but are not limited to, Lys-Phe-X, Lys-Val-Cit-PAB-X, NH2—(CH2CH2O)n-Val-Cit-PAB-X, and NH2—(CH2CH2O)n-(Val-Cit-PAB-X)2, wherein X is the active moiety, and n is an integer of at least 1 (e.g., 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, or more)” (paragraph 0172 of the pre-grant publication).
WALSH is directed to antibody–drug conjugates (ADCs) which harness the highly specific targeting capabilities of an antibody to deliver a cytotoxic payload to specific cell types and have garnered widespread interest in drug discovery, particularly in oncology, as discrimination between healthy and malignant tissues or cells can be achieved. See abstract. WALSH teaches that antibody–oligonucleotide conjugates are related biologics. See p. 1333, left column, first sentence.
WALSH teaches that a promising strategy for site-specific native antibody conjugation has emerged, involving the use of small protein domains or peptides that non-covalently bind to a conserved sequence in the antibody Fc domain with high affinity. WALSH teaches a 13-residue peptide (called Fc-III) was identified as binding the Fc region of IgG antibodies and that incorporation of para-benzoyl-phenylalanine (BPA) into the Fc-III peptide enabled covalent modification of HC-M252 in trastuzumab upon irradiation with ultraviolet light. See 2.6.5 Affinity peptide labelling, p. 1326 - 1327 and Fig. 15A, p. 1327. Thus, WALSH teaches B of Formula I of present claim 76.
WALSH teaches various conjugation sites on an antibody. See Fig. 3, p. 1308. Thus, WALSH teaches A-C1 of Formula I of present claim 76.
WALSH teaches the therapeutic agent MMAE attached to the trastuzumab through a PEG24 spacer and a cleavable Val-Cit-PABC motif. See p. 1313, left column, second paragraph; p. 1314, left column; and Figs. 7, 9. WALSH further teaches trastuzumab ADC containing MMAE and a b-galactosidase-cleavable linker (see p. 1318, left column, second paragraph). Thus, like DUGAL-TESSIER (see discussion above), WALSH teaches A-C1-L1-P1-D of Formula I of present claim 76.
WALSH teaches multiple conjugation sites on the targeting moiety (antibody) of the ADC. See Fig. 3.
Regarding claim 76, because DUGAL-TESSIER teaches an antibody oligonucleotide conjugate with a cleavage site, conjugation site, linker, and oligonucleotide (as discussed above), and thus teaches P2-C2-L2-O of Formula I, and WALSH teaches B-A-C1-L1-P1-D, it would have been obvious to combine the references to arrive to the structure of Formula I of present claim 76. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05(II)(A).
Regarding claims 77 – 79, WALSH teaches that a ‘cleavable’ linker is employed, in which a chemical- (e.g. low pH or glutathione) or enzyme- (e.g. protease, phosphatase, glycosidase or sulfatase5) sensitive trigger is incorporated. See p. 1306, top of right column.
Regarding claim 81, WALSH teaches Trop-2-targeting ADC. See p. 1313-left col. and p. 1333-right column.
Regarding claims 88 and 90, DUGAL-TESSIER teaches ionic conjugation to deliver multiple siRNA sequences in one construct which implies a plurality of targeting conjugates. Furthermore, DUGAL-TESSIER teaches that AOC was dosed to deliver 3 - 80 micrograms of siRNA both intratumorally and intravenously (see p. 13, 4.2. Efficacy, second paragraph) and thus teaches a pharmaceutical composition of the AOC.
Claims 81 – 85, 86 and 91 are rejected under 35 U.S.C. 103 as being unpatentable over DUGAL-TESSIER in view of WALSH as applied to claims 75 – 79, 81, and 88 – 90, and further in view of AJINOMOTO.
The teachings of DUGAL-TESSIER and WALSH is discussed above and fully incorporated here.
According to the present specification, “the TBF non-covalently binds to the targeting moiety. In some embodiments, the targeting moiety binding peptide is an antibody binding peptide (‘ABP’), which is a polypeptide that specifically binds to an antibody. Exemplary ABPs include, but are not limited to, an FcBP-1, an FcBP-2, an Fc-III and fragments thereof. As used herein, a TBF comprising an ABP is referred herein as an ‘antibody binding fragment’ or ‘ABF’ “ (paragraph 0096 of the pre-grant publication).
Regarding claim 80, AJINOMOTO teaches a polypeptide having an affinity for an antibody (p. 8, fifth line from the bottom) and that an affinity polypeptide for the antibody is a peptide Fc-III consisting of the amino acid sequence of DCAWHLGELVWCT (SEQ ID NO: 54), which has been reported to have the ability to bind to human IgG (see p. 27, sixth paragraph). AJINOMOTO’s SEQ ID NO: 54 is identical to present SEQ ID NO: 75 of present claim 80. See Appendix.
Because DUGAL-TESSIER in view of WALSH teaches the structure of Formula I of present claim 76 and AJINOMOTO teaches an antibody affinity polypeptide (which is interpreted to be B (TBF) of Formula I of present claim 76) having the sequence of present SEQ ID NO: 75, it would have been obvious to modify the structure rendered obvious by DUGAL-TESSIER and WALSH with AJINOMOTO’s affinity polypeptide to arrive to the invention of claim 80. There would have been a reasonable expectation of success considering that the components and production of Formula I is known in the art, as evidenced by the cited references.
Regarding claims 81 – 83, AJINOMOTO teaches that the antibody is bispecific (see p. 23, second paragraph) and that the protein that is the antigen of the antibody may be a disease target protein such as PD-L1 (a checkpoint factor) or Trop2 (see p. 24, eighth paragraph).
Thus, because DUGAL-TESSIER teaches the targeting conjugate of present claim 75 and AJINOMOTO teaches targeting conjugate with an anti-PD-L1 or anti-Trop-2 antibody and a bispecific antibody, it would have been obvious to modify DUGAL-TESSIER’s targeting conjugate with AJINOMOTO’s antibody to arrive to the invention of present claims 81 – 83. There would have been a reasonable expectation of success considering that an AOCs are known in to deliver antibodies in the treatment of cancer and considering that PD-L1 and Trop-2 are cancer antigens that are targeted by antibodies in cancer treatments, as evidenced by the applied prior art.
Regarding claim 84, AJINOMOTO teaches that a monoclonal antibody is a full-length antibody or an antibody fragment (eg, F (ab ′) 2 , Fab ′, Fab, Fv, single chain antibody) (see p. 24, fourth paragraph) and may be a bispecific antibody (see p. 23, second paragraph). Thus, it would have been obvious to that A comprises a full-length antibody recognizing a first target molecule, an scFv, sdAb, or scFab recognizing a second target molecule, and the optional third cleavage site.
Regarding claim 85, AJINOMOTO teaches that the antigen of the antibody may be a disease target protein such as PD-L1 (see p. 24, eighth paragraph).
Regarding claim 86, AJINOMOTO teaches formula (III ′): AB-2 '(-F2) -L'-B1' (-F1) -R'-T (III ') where A is an affinity substance for the antibody, R' is a moiety generated by the reaction between the antibody and the reactive group, T is an antibody. L' is a cleavable linker that is a divalent group containing a cleavable moiety, B1 ′ and B2 ′ are the same or different and each is a trivalent group containing a moiety generated by a reaction between a functional substance and a bioorthogonal functional group, F1 and F2 are the same or different and are functional substances. See p. 17, [20].
According to AJINOMOTO, functional substances may be drugs, auristatin (MMAE, MMAF) or oligonucleotides and that the functional substance may also be a single functional substance or a substance in which two or more functional substances are linked. See 3-2. Functional substance (F), p. 45 – 46.
Thus, AJINOMOTO renders (e) a first therapeutic agent conjugated to the first conjugation site via a first linker; (f) a second therapeutic agent conjugated to the second conjugation site via a second linker; (g) a first oligonucleotide conjugated to the first polypeptide chain via a third linker; and (h) a second oligonucleotide conjugated to the second polypeptide chain via a fourth linker of present claim 86 obvious.
WALSH teaches conjugation sites on each of the heavy chains of the antibody (see Fig. 3, p. 1308) and thus renders a first antibody heavy chain, a first conjugation site, and a first scFv, scFab, or sdAb; (b) a second polypeptide chain comprising from N terminus to C terminus: a second antibody heavy chain, a second conjugation site, and a second scFv, scFab, or sdAb; (c) a third polypeptide chain comprising a first antibody light chain; (d) a fourth polypeptide chain comprising a second antibody light chain obvious.
Overall, it would have been obvious to modify DUGAL-TESSIER’s AOC with WALSH’s conjugation sites to conjugate a first and a second therapeutic agent and a first and a second oligonucleotide to arrive to the invention of present claim 86. There would have been a reasonable expectation of success considering that similar variations of the claimed targeting conjugate are known to effectively treat diseases, as evidenced by the applied prior art.
Regarding claim 91, according to the present specification Formula (3) has the structure (Glycine)3-(PEG)4-VC-PAB-MMAE (paragraph 0176 of the pre-grant publication). WALSH teaches that DBCO-PEG3-Val-Cit-PABC-MMAE payloads generated ADCs with no significant change in binding observed, and no loss in stability (see p. 1333, left column, second paragraph). Furthermore, WALSH teaches that penta-glycine tagged payloads containing maytansine or MMAE generate homogeneous ADCs with conjugation of the payload to the antibody having no adverse effect on the antigen binding and with reaction efficiencies exceeding 80% (see p. 1335, right column). Because WALSH teaches all the components of Formula (3): (Glycine)3-(PEG)4-VC-PAB-MMAE, it would have been obvious to arrive to the formula with the teachings of WALSH via routine experimentation. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05(II)(A).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 75 – 91 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 59 – 80 of copending Application No. 18/278,787 in view of DUGAL-TESSIER, AJINOMOTO, and WALSH.
Copending claim 59 recites a targeting conjugate comprising a targeting moiety and an effector molecule, wherein the targeting moiety specifically binds to a target molecule, wherein the effector molecule is conjugated to the targeting moiety via a conjugation site, and wherein the effector molecule can be released from the targeting conjugate via cleavage.
Copending claim 65 recites a targeting conjugate of claim 59, wherein the effector molecule is selected from the group consisting of a therapeutic agent, an oligonucleotide, and a detectable label.
The main difference between the present claims and the copending claims is that the present claims recite a targeting conjugate having components with a different connectivity (present claim 76). However, DUGAL-TESSIER, AJINOMOTO, and WALSH teach these differences. The teachings of DUGAL-TESSIER, AJINOMOTO, and WALSH, and how they relate to the claims, are set forth in the rejections under 35 U.S.C. 102 and 103 above.
Because the copending claims recites a targeting conjugate comprising a targeting moiety, and DUGAL-TESSIER, AJINOMOTO, and WALSH teach different ways to connect the of the components of the targeting moiety of the copending claims, it would have been obvious to one having ordinary skill in the art to use the components of the copending claims’ conjugate to arrive to the conjugate of the present claims. There would have been a reasonable expectation of success considering that the claimed structure of the targeting conjugate has components known in ADCs and AOCs that have been successful in treating diseases.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Estella Gustilo whose telephone number is (703)756-1706. The examiner can normally be reached Monday - Friday 9:30 AM - 5:30 PM.
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/ESTELLA M. GUSTILO/Examiner, Art Unit 1646
/PETER J REDDIG/Primary Examiner, Art Unit 1646
APPENDIX
Alignment with SEQ ID NO: 75
BHT52112
ID BHT52112 standard; peptide; 13 AA.
XX
AC BHT52112;
XX
DT 25-JUN-2020 (first entry)
XX
DE Human IgG Fc region affinity polypeptide (Fc-III), SEQ ID 54.
XX
KW Fc-III protein; Immunoglobulin; antibody production; immunoconjugate.
XX
OS Unidentified.
XX
CC PN WO2020090979-A1.
XX
CC PD 07-MAY-2020.
XX
CC PF 31-OCT-2019; 2019WO-JP042785.
XX
PR 31-OCT-2018; 2018JP-00205225.
XX
CC PA (AJIN ) AJINOMOTO CO INC.
XX
CC PI Yamada K, Matsuda Y, Takahashi K, Shikida N, Shimbo K, Nagano H;
XX
DR WPI; 2020-37501K/041.
XX
CC PT New protein compound or its salt having affinity substance for antibody,
CC PT cleavable moiety and reactive group, useful in regioselective modifying
CC PT reagent for producing antibody having bioorthogonal functional group.
XX
CC PS Example 2; SEQ ID NO 54; 273pp; Japanese.
XX
CC The present invention relates to a novel compound useful for producing an
CC antibody having a bioorthogonal functional group. The novel compound
CC comprises a substance with affinity for an antibody corresponds to SEQ ID
CC NOs: 7-10, 22-25 and 51-53 (see BHT52065-BHT52068, BHT52080-BHT52083 and
CC BHT52109-BHT52111), a cleavable linker, a divalent group containing the
CC bioorthogonal functional group and a reactive group for the antibody. The
CC invention further provides: a regioselective modifying reagent comprising
CC the compound (antibody drug complex (ADC)); and a method for producing
CC the antibody having the bioorthogonal functional group or its salt.
XX
SQ Sequence 13 AA;
ALIGNMENT:
Query Match 100.0%; Score 86; Length 13;
Best Local Similarity 100.0%;
Matches 13; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DCAWHLGELVWCT 13
|||||||||||||
Db 1 DCAWHLGELVWCT 13