The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
This office action is in response to Applicants’ remarks received September 16, 2025.
As an initial matter, and as previously noted, in the claim set filed May 5, 2025, claims 2-5 do not have the correct status identifiers. As noted in the April 30, 2025 interview summary, claims 2-5 were canceled in a preliminary amendment filed October 1, 2021. Applicants are requested to submit an amended claim set indicating claims 2-5 are canceled. The restriction requirement inadvertently included claims 2-5 because the text of the claims were presented in the preliminary amendment. MPEP 714 notes that a claim being canceled must be indicated as “canceled;” the text of the claim must not be presented. A canceled claim can be reinstated only by a subsequent amendment presenting the claim as a new claim with a new claim number. The original numbering of the claims must be preserved throughout the prosecution. When claims are canceled, the remaining claims must not be renumbered. For example, when applicant cancels all of the claims in the original specification and adds a new set of claims, the claim listing must include all of the canceled claims with the status identifier (canceled) (the canceled claims may be aggregated into one statement). The new claims must be numbered consecutively beginning with the number next following the highest numbered claim previously presented (whether entered or not) in compliance with 37 CFR 1.126.
Claims 7-8 correspond to original claims 4-5.
Claims 2-5 are considered to be canceled for the purposes of this office action. Claims 1, 6 are withdrawn. Claims 7-8 are under consideration.
Priority: The instant application has a benefit date of October 1, 2021.
Objections and Rejections
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.
Claim 7 is rejected under 35 U.S.C. 103 as being unpatentable over Mukhopadhayay et al. (2020 Biomacromolecules 21: 867-877; previously cited) in view of Perriman et al. (2010 Nature Chemistry 2(8): 622-626; previously cited) and McDaniel (US 20100233146; previously cited). Mukhopadhayay et al. disclose that under chemical and thermal stresses, the structure of alpha-CT (chymotrypsin) can be easily perturbed and unfolded leading to formation of inactive fibrillar aggregates, thereby preventing its application in industrial processes (at least p. 870). Mukhopadhayay et al. disclose that moreover, the use of organic solvents can be deleterious to the functionality of alpha-CT, thus preventing its use in nonaqueous conditions required for the industrial processes (at least p. 870). Mukhopadhayay et al. disclose that therefore, stabilizing alpha-CT in nonaqueous and under green environment conditions can be highly beneficial (at least p. 870). Mukhopadhayay et al. disclose preparing a waterless alpha-CT polymer surfactant bioconjugate comprising covalently linking DMAPA to native alpha-CT by the carbodiimide (EDC) mediated activation method to obtain cationized alpha-CT, coupling the cationized alpha-CT with anionic polymer surfactant (glycolic acid ethoxylate lauryl ether), mixing and dialyzing to obtain a polymer-surfactant conjugated cationized-alpha-CT, lyophilizing the polymer-surfactant conjugated cationized-alpha-CT to obtain a low density powder, which when annealed in an oven yielded a waterless protein polymer surfactant bioconjugate system (at least p. 869). Mukhopadhayay et al. disclose that the water-less alpha-CT polymer surfactant bioconjugate was prepared from known procedures for other types of proteins, citing at least ref. 9 to Perriman et al. 2010 (at least p. 869, 876). Mukhopadhayay et al. do not explicitly teach poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether or incorporating the waterless alpha-CT polymer surfactant bioconjugate with a thermoplastic adhesive.
Perriman et al. disclose preparing a solvent-free protein liquid, where the anionic polymer surfactants for binding to the cationized biomolecules are poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether or glycolic acid ethoxylate lauryl ether (at least p. 622).
McDaniel discloses compositions and/or materials, including a coating, an elastomer, an adhesive, etc., comprising an active enzyme including esterase, antimicrobial peptide, lysozyme, and/or peptidase, among others (at least abstract, paragraphs 0003-0010, p. 298-300 claims 1, 12); where the enzyme is chymotrypsin (at least example 33, p. 300 claim 12); where the elastomer is a thermoplastic elastomer (at least paragraphs 1085-1115, 1137-1155), including blends of thermoplastic adhesive and/or elastomeric adhesive (at least paragraphs 1165-1166, 1170-1172, 1177-1180,1196-1197, 1201-1204, 1207-1208, 1219-1224) and/or a protein adhesive (“protein glue”) (at least paragraphs 1225-1226) (also p. 304 claims 76-77, 78-79). McDaniel discloses that an adhesive typically comprises a solid or a liquid, but converts into a solid final form ("set") during normal use with desired attachment and material strength properties. For example, a liquid adhesive typically solidifies via a mechanism such as curing (i.e., a chemical reaction), cooling if molten, liquid component loss ( e.g., evaporation, heating), or a combination thereof; while a solid adhesive may cure into a final solid form, or already be in a solid final form (e.g., a pressure sensitive adhesive) (at least paragraph 1156). McDaniel discloses that the proteinaceous molecule (e.g. peptide) and/or property of the proteinaceous molecule may be stabilized in a material formulation by immobilization (e.g. attachment, linking, tethering, and/or conjugation) to another molecule; for example conjugated, chemically linked, tethered to a carrier molecule, including polymers (at least paragraph 0528).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine the references and arrive at the claimed method for making a chymotrypsin protein liquid/thermoplastic material comprising mixing cationized chymotrypsin and anions of poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether to form a cationized chymotrypsin-anion complex; lyophilizing and melting the cationized chymotrypsin-anion complex to form a water-free chymotrypsin ionic liquid; blending the chymotrypsin ionic liquid with a molten thermoplastic adhesive (“hot glue”); and cooling to create a proteolytic thermoplastic adhesive (glue) (instant claim 7). The motivation to do so is given by the prior art. Mukhopadhayay et al. disclose proteins, including chymotrypsin, can be stabilized in a water-less protein polymer surfactant bioconjugate system for industrial processes. Perriman et al. disclose polymers for the waterless protein polymer surfactant bioconjugate system of Mukhopadhayay et al. include poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether. McDaniel discloses industrial and commercial use of proteins and enzymes, including chymotrypsin, in compositions and/or materials including an elastomer, adhesive, including blends of thermoplastic adhesive and/or elastomeric adhesive and/or protein adhesive. Therefore, one of ordinary skill would have reasonable motivation to incorporate the poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether of Perriman et al. for the anionic polymer in the method for forming the water-less alpha-CT polymer surfactant bioconjugate system of Mukhopadhayay et al. and to further incorporate the water-less alpha-CT polymer surfactant bioconjugate system into a thermoplastic adhesive blend (or “glue”) as suggested in McDaniel because there was interest in stabilizing proteins and enzymes, such as chymotrypsin, for industrial use in thermoplastic/adhesive materials. One of ordinary skill would have a reasonable expectation of success because the prior art discloses waterless protein polymer surfactant bioconjugates systems stabilize proteins for various uses in industry.
Reply: Applicants’ remarks have been considered but they are not persuasive.
Applicants assert that the examiner does not provide analysis of how and why a skilled artisan would have combined the methods and chemicals of the prior art, in the manner in which the currently presented claims suggest, fails the requirements for the examiner to provide reasoned statements as to the motivation and basis of a reasonable expectation of success as required by the Federal Circuit.
Applicants’ remarks are not persuasive. As noted in the 103 rejection above, Mukhopadhayay et al. disclose proteins, including chymotrypsin, can be stabilized in a water-less protein polymer surfactant bioconjugate system for industrial processes (p. 869, 876). Perriman et al. disclose polymers for the waterless protein polymer surfactant bioconjugate system of Mukhopadhayay et al. include poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether (p. 622). McDaniel discloses industrial and commercial use of proteins and enzymes, including chymotrypsin, in compositions and/or materials including an elastomer, adhesive, including blends of thermoplastic adhesive and/or elastomeric adhesive and/or protein adhesive (see above).
Therefore, one of ordinary skill would have reasonable motivation to incorporate the poly(ethylene glycol) 4-nonylphenyl 3-sulfopropyl ether of Perriman et al. for the anionic polymer in the method for forming the water-less alpha-CT polymer surfactant bioconjugate system of Mukhopadhayay et al. and to further incorporate the water-less alpha-CT polymer surfactant bioconjugate system into a thermoplastic adhesive blend (or “glue”) as suggested in McDaniel because there was interest in stabilizing proteins and enzymes, such as chymotrypsin, for industrial use in thermoplastic/adhesive materials. One of ordinary skill would have a reasonable expectation of success because the prior art discloses waterless protein polymer surfactant bioconjugates systems stabilize proteins for various uses in industry.
Therefore, the 103 rejection adequately provides motivation to combine the references and a reasonable expectation of success to thereby arrive at the claimed method.
Claims 7-8 are rejected under 35 U.S.C. 103 as being unpatentable over Mukhopadhayay et al. (2020 Biomacromolecules 21: 867-877; previously cited) in view of Perriman et al. (2010 Nature Chemistry 2(8): 622-626; previously cited), McDaniel (US 20100233146; previously cited), and Liu et al. (2014 WIRES Nanomed Nanobiotechnol 5: 599-614; previously cited). The teachings of Mukhopadhayay et al., Perriman et al., and McDaniel over instant claim 7 are noted above.
Regarding instant claim 8, McDaniel discloses that in some embodiments, the proteinaceous composition further comprises a carrier (e.g. microsphere, liposome, etc.) (at least paragraphs 0303, 0529) and/or fillers selected from among a microsphere, a nanofiller, nanotube (at least paragraphs 1305, 1311, 1312-1314). Liu et al. disclose that materials and/or polymers having antifouling properties are critical to many biomedical and engineering applications such as medical implants and coatings (at least p. 599). Liu et al. disclose that antifouling polymers have been widely used to modify nanoparticles, such as gold nanoparticles, gold nanorods, quantum dots, magnetic particles, polymer particles, liposomes, etc. to improve their stability in ionic solutions, protein solutions, complex media, for in vitro or in vivo biomedical applications (at least p. 604-605). It would have been obvious to one of ordinary skill to further blend one or more of the gold nanorods and quantum dots disclosed in Liu et al. with the chymotrypsin ionic liquid blended with a molten thermoplastic adhesive (“hot glue”) in the method of Mukhopadhayay et al., Perriman et al. and McDaniel noted above. The motivation to do so is given by the prior art, which disclose that materials and/or polymers having functionalized properties can be blended or combined with nanomaterials for uses in industry and biomedical applications.
Reply: Applicants’ remarks are not persuasive. As noted above, the 103 rejection adequately provides motivation to combine the references and a reasonable expectation of success to thereby arrive at the claimed method. McDaniel discloses incorporating carriers and/or fillers into the proteinaceous composition (see above), where known carriers and fillers include nanoparticles, nanotubes, quantum dots, etc. (McDaniel; Liu et al.) for incorporation into polymer compositions to improve their stability in ionic solutions, protein solutions, complex media, for in vitro or in vivo biomedical applications (Liu et al.).
No claim is allowed.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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.
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/Marsha Tsay/Primary Examiner, Art Unit 1656