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 .
Claims 82-99 are pending.
Applicant’s election without traverse of Group I that read on (A) ADC-1 having the following structure
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in claim 94, (B) D is P2 having the following structure
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, which is the second compound in claim 87, (C) -L-D having the following structure
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in claim 88 and (D) Ab-L-D having the following structure
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in claim 89, in the reply filed on March 13, 2026 is acknowledged.
Claims 84 and 96-99 are withdrawn from further consideration by the examiner, 37 C.F.R. 1.142(b) as being drawn to non-elected inventions.
Claims 82-83 and 85-95, drawn to a drug conjugate that read on (A) ADC-1 having the following structure
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in claim 94, (B) D is P2 having the following structure
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, which is the second compound in claim 87, (C) -L-D having the following structure
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in claim 88 and (D) Ab-L-D having the following structure
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in claim 89, are being acted upon in this Office Action.
Priority
Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on March 13, 2026 and Oct 30, 2025 have been considered by the examiner and an initialed copy of the IDS is included with this Office Action.
Drawings
The drawings filed on Oct 30, 2025 are acceptable.
Specification
The substitute specification filed on Oct 31, 2025 has been entered.
The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant's cooperation is requested in correcting any errors of which applicant may become aware in the specification.
Claim Objection
Claim 86 is objected to because of the following informality: “or the following groups” should be deleted.
Claim 90 is objected to because of the following informality: “selected from” should have been “selected from the group consisting of”.
Claim 92 is objected to because of the following informalities:
the claim uses the abbreviation DAR without first defining it. To clarify the claim, applicant should first spell out the full term before using an abbreviation. Given the subject matter of the specification, the examiner presumes that "DAR" stands for "Drug Antibody Ratio".
“2-8” should have been “2 to 8”. Appropriate correction is required.
Claim 93 is objected to because of the following informality: the dash line in “3-4, 3.8-4.2, 3-5, 4-5.5, 5-7, 6.5-8 or 6-8” should have been “to”.
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.
Claim 82 is 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 applicant regards as the invention.
Regarding claim 82, the phrase "i.e.," renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claim rejections under - 35 U.S.C. 112
The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
Claims 82-83 and 85-95 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
The Written Description Guidelines for examination of patent applications indicates, “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, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical characteristics and/or other chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show applicant was in possession of the claimed genus.” (see MPEP 2163).
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The specification exemplifies:
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However, neither the specification nor the art teaches the broad genus of any drug conjugate comprising just 1, 2, 3, 4 or 5 CDRs of trastuzumab or just heavy chain variable region without the light chain variable region or vice versa or just heavy chain without the light chain or just light chain without the heavy chain of trastuzumab (claim 82) conjugated to any compound via linker comprises Mc-Val-Cit-PAB having the structure
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still maintains antigen binding to HER2 for treating any cancer.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRS (all six CDRs) in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. The specification provides no working examples showing that fewer than all six CDRs of the antibody or just heavy chain variable region or just light chain variable region or just heavy chain or just light chain of the antibody are required for binding to HER2 encompassed by the claimed conjugate. It is unlikely that an antibody as defined by claim 1, which may contain less the full complement of six CDRs from the heavy and light chain variable regions have the require binding function.
Chiu et al (Antibodies 8: 55-80, 2019; PTO 892) teaches the amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity, which is characteristic of the immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (see p. 4, in particular). As such, any drug conjugate comprising just one, two, three, four or five CDRs from trastuzumab or just heavy chain variable region without the light chain variable region or vice versa or just heavy chain without the light chain or vice versa cannot bind HER2, much less for use to target the drug to cell expressing HER2 to inhibit cell proliferation in vitro or in vivo.
Regarding any salt or solvate or racemic mixture or enantiomer or diastereomer or tautomer thereof (claim 82), tautomers are isomers that can exist in different configuration which can affect the drug’s stability and efficacy. Enantiomers are stereoisomers that differ in configuration but have the same molecular structure, which can influence drug behavior. Diasteromers are stereoisomers that differ in configuration but have the same molecule structure, which can affect drug metabolism and distribution. Racemates are mixtures of enantiomers, which can be used to improve the drug’s stability and efficacy.
However, there is no objective evidence of any drug conjugate salt or solvate or racemic mixture or enantiomer or diastereomer or tautomer thereof effective for treating disease such as any cancer or autoimmune disease.
Dhaked (Expert Opin Drug Discov 19(9): 1011-1016, 2024; PTO 892) teaches that Different tautomers can be metabolized by enzymes or converted non-enzymatically at different rates, see p. 2, in particular. Tautomerism can affect the binding of a drug to its target and the subsequent drug action, including the drug’s efficacy and potency, see p. 1011, left, in particular. Designing a molecule for targets of CNS diseases presents significant challenges as the BBB restricts the migration of molecules to the brain more strongly than to other body compartments. If the designed molecule is amenable to tautomerism, it may have multiple forms under physiological conditions. It should be present in sufficient amounts or exclusively to allow entry of the predominant tautomer, see p. 1013, right column, in particular. Dhaked teaches that currently, there are no computational tools or databases that provide information about ratios of different tautomers in aqueous solutions or other environments important for drug development. Selecting a suitable tautomer is crucial for understanding a drug molecule’s binding behavior including by docking, pharmacophore mapping, 3D-QSAR, and molecular dynamics simulation. Very fast tautomerization does not allow the separation of tautomers for clinical testing. On the other hand, half-life of tautomerization in the range of months has an impact on the formulation perspective, i.e., shelf-life of drugs. Epimerization may lead to minor tautomers as impurities if not detected during early studies. Lack of information on tautomeric preferences may affect the optimization of leads, development of a drug, its stability, drug product performance, formulation development, dose, bioavailability, manufacturing, shelf-life, and possible adverse effects and toxicities, see p. 1014-1015. There are no in vivo working examples. It is unpredictable which racemic mixture or enantiomer or diastereomer or tautomer of drug conjugated to anti-HER2 antibody is effective in vivo for treating any and all possible cancer and autoimmune disease. There are no in vivo working examples. One of skill in the art would not immediately envision or recognize which salt, racemic mixture or enantiomer or diastereomer or tautomer of drug conjugated to anti-HER2 antibody is effective in vivo for treating any and all possible cancer and autoimmune disease.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the written description inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116.).
Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddles v. Baird, 30 USPQ2d 1481, 1483. In Fiddles v. Baird, claims directed to mammalian FGF’s were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence. Thus, the specification fails to describe these DNA sequences.
For genus claims, an adequate written description of a claimed genus requires more than a generic statement of an invention's boundaries. A patent must set forth either a representative number of species falling within the scope of the genus or structural features common to the members of the genus. Kubin, Exparte, 83 USPQ2d 1410 (Bd. Pat. App. & Int. 2007); Ariad Pharms., Inc. v. Eli Lilly& Co., 598 F.3d 1336, 1350 (Fed. Cir. 2010).
Therefore, only an antibody drug conjugate having a structure represented by formula (I): Ab-(L-D)p, wherein the Ab is an anti-HER2 antibody trastuzumab or an antigen binding fragment thereof comprising a heavy chain CDRs 1-3 of SEQ ID NO: 1 to 3, respectively, and a light chain CDRs 1-3 of SEQ ID NO: 4-6, respectively, or a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 7 and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 8 or a heavy chain comprising the amino acid sequence of SEQ ID NO: 9 and a light chain comprising the amino acid sequence of SEQ ID NO: 10, wherein the L-D is
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and wherein the p is an integer from 1 to 4 for treating HER2 expressing cancer, (2) the antibody drug conjugate above having the structure of ADC-1, ADC-6 as shown in claim 94, and a pharmaceutical composition comprising the antibody drug conjugate above and a pharmaceutically acceptable carrier for treating HER2 expressing breast ductal carcinoma, but not the full breadth of the claims meets the written description provision of 35 U.S.C. § 112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. § 112 is severable from its enablement provision (see page 1115).
Claims 82-83 and 85-95 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for an antibody drug conjugate having a structure represented by formula (I): Ab-(L-D)p, wherein the Ab is an anti-HER2 antibody trastuzumab or an antigen binding fragment thereof comprising a heavy chain CDRs 1-3 of SEQ ID NO: 1 to 3, respectively, and a light chain CDRs 1-3 of SEQ ID NO: 4-6, respectively, or a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 7 and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 8 or a heavy chain comprising the amino acid sequence of SEQ ID NO: 9 and a light chain comprising the amino acid sequence of SEQ ID NO: 10, wherein the L-D is
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and wherein the p is an integer from 1 to 4 for treating HER2 expressing cancer, (2) the antibody drug conjugate above having the structure of ADC-1 or ADC-6 as shown in claim 94, and a pharmaceutical composition comprising the antibody drug conjugate above and a pharmaceutically acceptable carrier for treating HER2 expressing breast ductal carcinoma, does not reasonably provide enablement for the claimed drug conjugate having a structure represented by formula I: Ab-(L-D)p or any acceptable thereof, any solvate, racemic mixture, enationmer, diasteromer or tautomer thereof in which recites 1, 2, 3, 4 or 5 CDRs of trastuzumab, or just 1, 2 and 3 CDRs of the heavy chain variable region, or just HCDR1, HCDR2 and HCDR3 of trastuzumab or just 1, 2 and 3 CDRs of the light chain variable region or just LCDR1, LCDR2 and LCDR3 of trastuzumab or just heavy chain variable region of trastuzumab or just a light chain variable region of trastuzumab or just heavy chain of trastuzumab or just light chain of trastuzumab linked to (L-D)p and the structure of D. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Enablement is considered in view of the Wands factors (MPEP 2164.01(a)). These factors include, but are not limited to: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. . In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
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The specification exemplifies:
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However, enablement is not commensurate in scope with claims as how to make and use the broad genus of any drug conjugate comprising just 1, 2, 3, 4 or 5 CDRs of trastuzumab or just heavy chain variable region or just light chain variable region or just heavy chain or just light chain of trastuzumab (claim 82) conjugated to any compound via linker comprises Mc-Val-Cit-PAB having the structure
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still maintains antigen binding to HER2 for treating any cancer.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRS (all six CDRs) in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. The specification provides no working examples showing that fewer than all six CDRs of the antibody or just heavy chain variable region or just light chain variable region or just heavy chain or just light chain of the antibody are required for binding to HER2 encompassed by the claimed conjugate. It is unlikely that an antibody as defined by claim 1, which may contain less the full complement of six CDRs from the heavy and light chain variable regions have the require binding function.
Chiu et al (Antibodies 8: 55-80, 2019; PTO 892) teaches the amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity, which is characteristic of the immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (see p. 4, in particular). As such, any drug conjugate comprising just one, two, three, four or five CDRs from trastuzumab or just heavy chain variable region without the light chain variable region or vice versa or just heavy chain without the light chain or vice versa cannot bind HER2, much less for use to target the drug to cell expressing HER2 to inhibit cell proliferation in vitro or in vivo.
Regarding any salt or solvate or racemic mixture or enantiomer or diastereomer or tautomer thereof (claim 82), tautomers are isomers that can exist in different configuration which can affect the drug’s stability and efficacy. Enantiomers are stereoisomers that differ in configuration but have the same molecular structure, which can influence drug behavior. Diasteromers are stereoisomers that differ in configuration but have the same molecule structure, which can affect drug metabolism and distribution. Racemates are mixtures of enantiomers, which can be used to improve the drug’s stability and efficacy.
However, there is no objective evidence of any drug conjugate salt or solvate or racemic mixture or enantiomer or diastereomer or tautomer thereof effective for treating disease such as any cancer or autoimmune disease.
Dhaked (Expert Opin Drug Discov 19(9): 1011-1016, 2024; PTO 892) teaches that Different tautomers can be metabolized by enzymes or converted non-enzymatically at different rates, see p. 2, in particular. Tautomerism can affect the binding of a drug to its target and the subsequent drug action, including the drug’s efficacy and potency, see p. 1011, left, in particular. Designing a molecule for targets of CNS diseases presents significant challenges as the BBB restricts the migration of molecules to the brain more strongly than to other body compartments. If the designed molecule is amenable to tautomerism, it may have multiple forms under physiological conditions. It should be present in sufficient amounts or exclusively to allow entry of the predominant tautomer, see p. 1013, right column, in particular. Dhaked teaches that currently, there are no computational tools or databases that provide information about ratios of different tautomers in aqueous solutions or other environments important for drug development. Selecting a suitable tautomer is crucial for understanding a drug molecule’s binding behavior including by docking, pharmacophore mapping, 3D-QSAR, and molecular dynamics simulation. Very fast tautomerization does not allow the separation of tautomers for clinical testing. On the other hand, half-life of tautomerization in the range of months has an impact on the formulation perspective, i.e., shelf-life of drugs. Epimerization may lead to minor tautomers as impurities if not detected during early studies. Lack of information on tautomeric preferences may affect the optimization of leads, development of a drug, its stability, drug product performance, formulation development, dose, bioavailability, manufacturing, shelf-life, and possible adverse effects and toxicities, see p. 1014-1015. There are no in vivo working examples. It is unpredictable which salt, racemic mixture or enantiomer or diastereomer or tautomer of drug conjugated to anti-HER2 antibody is effective in vivo for treating any and all possible cancer and autoimmune disease.
As such, it would require undue experimentation of one skilled in the art to practice the claimed invention commensurate in scope with the claims. See page 1338, footnote 7 of Ex parte Aggarwal, 23 USPQ2d 1334 (PTO Bd. Pat App. & Inter. 1992).
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PHUONG HUYNH whose telephone number is (571)272-0846. The examiner can normally be reached on 9:00 a.m. to 6:30 p.m. The examiner can also be reached on alternate alternative Friday from 9:00 a.m. to 5:30 p.m.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Misook Yu, can be reached at 571-270-3497. The fax phone number for the organization where this application or proceeding is assigned is 571-272-0839.
Information regarding the status of an application may be obtained from Patent Center. Status information for published applications may be obtained from Patent Center. Status information for unpublished applications is available through Patent Center for authorized users only. Should you have questions about access to Patent Center, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
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) Form at https://www.uspto.gov/patents/uspto-automated- interview-request-air-form.
/PHUONG HUYNH/ Primary Examiner, Art Unit 1641
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
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