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 .
DETAILED ACTION
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office Action.
Status of Claims
Claims 1-14 are currently pending. Claims 1, 3, 6, 8 and 11 have been amended by Applicants’ amendment filed 07-14-2026. No claims have been added or canceled by Applicants’ amendment filed 07-14-2026.
Applicant's election with traverse of Group I, claims 1-6 and 11, directed to a method for screening for a polypeptide that acts on a target protein; and Applicant’s election with traverse of Species as follows:
Species (A): wherein the polypeptides comprise an amino acid sequence in which the predicted site is randomized in the amnio acid sequence of the ligand (claim 3), in the reply filed March 20, 2026 was previously acknowledged.
Claims 7, 8-10 and 12-14 were previously withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected invention, there being no allowable generic or linking claim.
Claims 5 and 11 were previously withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected species, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on March 20, 2026.
The restriction requirement was deemed proper and was made FINAL.
The claims will be examined insofar as they read on the elected species.
A complete reply to the final rejection must include cancellation of nonelected claims or other appropriate action (37 CFR 1.144) See MPEP § 821.01.
Therefore, claims 1-4 and 6 are under consideration to which the following grounds of rejection are applicable.
Priority
The present application filed February 2, 2023, claims the benefit of a 35 U.S.C. 371 national stage filing of International Application PCT/JP2021/028940, filed August 4, 2021, which claims the benefit Japanese Patent Application JP2020-132823, filed August 5, 2020.
Acknowledgment is made of Applicant's claim for foreign priority based on an application filed in the Japan on August 5, 2020, and of Applicant’s filing of the certified copy of Japanese Patent Application
JP2020-132823 on February 2, 2023 as required by 37 CFR 1.55.
Applicant’s filing of an English translation of JP2020-132823, in the reply filed 07-14-2026, is acknowledged. The Examiner requests that the certification document (e.g., the Verification of Translation), filed July 14, 2026 additionally comprise:
The language pair (source language and target language).
A statement that the translation is a true, completely, and accurate rendering of the source document.
A statement of the translator’s competency to translate between the two language, or a reference to their credential or certification body.
Interview Summary
Applicant contacted the Examiner to set up an interview, where such telephonic interview was conducted between the Examiner and Applicant’s representative Nicholas Rosa on June 25, 2026. Applicant’s proposed amendments to the claims, the 35 USC 112(b) rejections, and the 35 USC 103 rejection of record were discussed.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on June 9, 2026 and August 20, 2026 have been considered. Initialed copies of the IDSs accompany this Office Action.
Withdrawn Objections/Rejections
Applicants’ amendment and arguments filed July 14, 2026 are acknowledged and have been fully considered. The Examiner has re-weighed all the evidence of record. Any rejection and/or objection not specifically addressed below are herein withdrawn.
Claim Objections
The objection to claim 3 withdrawn due to Applicant spelling out the abbreviation, in the reply filed 07-14-2026.
Claim Rejections - 35 USC § 102
The rejection of claims 1-4 and 6 is withdrawn under 35 U.S.C. 102(a1)/102(a2) as being anticipated by Kubo et al. (hereinafter “Kubo”) (International Application WO2010104114A1, filed September 16, 2010, also JP2014207905A; and English Translation).
Kubo does not specifically exemplify a patch clam technique configured to measure current flow.
In view of the withdrawn rejection, Applicant’s argument is rendered moot.
Claim Rejections - 35 USC § 103
The rejection of claims 1-4 and 6 is withdrawn under 35 U.S.C. 103 as being unpatentable over Kubo et al. (hereinafter “Kubo”) (International Application WO2010104114A1, filed September 16, 2010, also JP2014207905A; and English Translation) in view of Fernandez-Recio et. al. (hereinafter “Fernandez-Recio”) (Proteins: Structure, Function, and Bioinformatics, 2005, 58, 134-143).
Kubo does not specifically exemplify a patch clam technique configured to measure current flow.
In view of the withdrawn rejection, Applicant’s argument is rendered moot.
Maintained Objections/Rejections
Claim Rejections - 35 USC § 112(b)
The rejection of claims 1-4 and 6 is maintained under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claim 1 is indefinite for the recitation of the term “the polypeptide” such as recited in claim 1, lines 8-9, 11, 14 and 16 because it is unclear whether the plurality of vectors that express “the polypeptide” are all expressing a single polypeptide, wherein all polypeptides having the same structure, or whether the plurality of vectors are intended to express a plurality of different polypeptides each comprising a different structure and, thus, the metes and bounds of the claim cannot be determined.
Claim 1 is indefinite for the recitation of the term “associated” in claim 1, line 15 because the term “associated” is relative term that renders the claim indefinite. The term “associated” is not defined by the claim, and the Specification does not provide a standard for ascertaining the requisite amount of association as compared to some other value that qualifies current flow as being “associated” with the target protein (e.g., current as compared to unbound target protein, etc.), such that one of ordinary skill in the art would not be reasonably appraised of the scope of the invention and, thus, the metes and bounds of the claim cannot be determined.
Claim 1 is indefinite for the recitation of the term “the measured antagonist activity or agonist activity” such as recited in claim 1, lines 16-17. There is insufficient antecedent basis for the term “the measured antagonist activity or agonist activity” in the claim. The Examiner suggests that Applicant amend claim 1 to recite, for example, “to measure an antagonist activity or agonist activity of the polypeptide to obtain a measured antagonist activity or agonist activity of the polypeptide.”
The rejection of claim 3 is indefinite for the recitation of the terms “ligand”, “one or more sites on the ligand”, “randomized in the amino acid sequence”, “applying ODA”, and “another protein” such as recited in claim 3, lines 4-5 because claim 3 depends from instant claim 1, wherein claim 1 does not recite the presence of ligands, one or more sites on ligands, analysis techniques or devices, and/or other proteins. Thus, it is unclear what ligand and/or other proteins are being referred to and, thus, the metes and bounds of the claim cannot be determined.
Claim 3 is indefinite for the recitation of the term “the predicted one or more sites” such as recited in claim 1, line 7. There is insufficient antecedent basis for the term “the predicted one or more sites” in the claim because claim 3, lines 4-5 recites the term “one or more sites on the ligand.”
Claim 3 is indefinite for the recitation of the term “preparing the polynucleotide library” such as recited in claim 1, line 9 because it is unclear how the recited steps of: ODA analysis of a ligand for a membrane protein, predicting one or more sites on the ligand that can interact with “another protein”, and preparing a plurality of polypeptides each having a sequence in which the predicted one or more sites on a ligand are randomized, prepares a polynucleotide library. Moreover, instant claim 1 recites a “polynucleotide library constituted of a plurality of expression vectors that can be expressed” in lines 3-4; however, claim 3 does not recite any polynucleotides (first, second, a plurality, etc.), expression vectors, bacterium, etc. such that it is completely unclear how polynucleotide library is prepared by the method recited in instant claim 3 and, thus, the metes and bounds of the claim cannot be determined.
Claim 6 is indefinite for the recitation of the term “increased” in claim 6, line 2 because the term “increased” is relative term that renders the claim indefinite. The term “increased” is not defined by the claim, and the Specification does not provide a standard for ascertaining the requisite amount of increase in concentration as compared to some other value that qualifies as an increase first polynucleotide concentration (e.g., as compared to a starting concentration), such that one of ordinary skill in the art would not be reasonably appraised of the scope of the invention and, thus, the metes and bounds of the claim cannot be determined.
Claim 6 is indefinite for the recitation of the term “increasing the concentration of the first polynucleotides” such as recited in claim 6, lines 2-3 because claim 6 depends from instant claim 1, wherein claim 1 does not recite that the polynucleotide library is present in a solution, solvent, liquid, etc., that the first polynucleotides are present in any specific concentration, and/or polynucleotides that encode polypeptides that bind to a target protein. It is unclear if the claim is referring to a step of “enriching” or enrichment of first polynucleotides and, thus, the metes and bounds of the claim cannot be determined.
Claims 2 and 4 are indefinite insofar as they ultimately depend from instant claim 1.
Claim Rejections - 35 USC § 112(d)
The rejection of claims 3 and 6 is maintained under 35 U.S.C. 112(d) as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 3 recites (in part): “applying an ODA analysis to a three-dimensional structure…preparing a polynucleotide library” in lines 3-9 because claim 3 depends from instant claim 1, wherein claim 1 does not recite the presence of any ligands, one or more predicted sites including randomized sites on a ligand, another protein, a 3D structure, etc. Moreover, claim 3 does not actually recite a method of preparing a polynucleotide library. Thus, claim 3 is an improper dependent claim for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 6 recites (in part): “further comprising prior to (1) increasing a concentration of the first polynucleotides…repeatedly selecting and amplifying the first polynucleotides” in lines 2-4 because claim 6 depends from instant claim 1, wherein claim 1 does not recite the presence of a solution, solvent, liquid, etc. and/or any specific concentration of first polynucleotides, and/or polypeptides that bind to a target protein. Thus, claim 6 is an improper dependent claim for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Applicant may cancel the claim, amend the claim to place the claim in proper dependent form, rewrite the claim in independent form, or present a sufficient showing that the dependent claim complies with the statutory requirements.
New Objections/Rejections
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 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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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 1-4 and 6 are rejected under 35 U.S.C. 103 as being unpatentable over Kubo et al. (hereinafter “Kubo”) (International Application WO2010104114A1, filed September 16, 2010; also, JP2014207905A; and English Machine Translation; of record) in view of Tadashi Kimura (hereinafter “Kimura”) (Journal of Bioanalysis & Biomedicine, 2017, 9(5), 263-268) as evidenced by Kimura et al. (hereinafter “Kimura and Kubo”) (Spider Venoms, Toxicology, 2015, Gopalakrishnakone, P., Corzo, G., Diego-Garcia, E., de Lima, M. (eds), Springer, Dordrecht, 1-16). This is a new rejection necessitated by amendment of the claims in the response filed 07-14-2026.
Regarding claim 1 (in part), Kubo teaches that the invention relates to methods of preparing polypeptide libraries and methods of using them to identify novel polypeptides (paragraph [0001]). Kubo teaches that the polypeptide library is prepared in which the amino acid sequences of regions involved in interaction (for example, loop regions) are designed to be random while maintaining the structure of the framework region of the protein; and the venoms that snakes, scorpions, spiders, and insects use for defense or attack against other organisms for immediate action are generally neurotoxins, which can rapidly paralyze them, wherein each of these organisms has several kinds of neurotoxins, among which polypeptide neurotoxins called "a -type neurotoxins" are often antagonists to voltage-gated ion channels (interpreted as antagonist activity, claim 1) (paragraph [0002], lines 25-29). Kubo teaches that conventionally developed polypeptide libraries can be used as a high-throughput screening system for agonists and antagonists including for the development of a high-throughput screening system targeting membrane proteins (paragraph [0003], lines 50-51 and 58-59). Kubo teaches a method for preparing a polypeptide having affinity for a target protein, the method comprising the following steps (a) to (e); (a) comprising a group of expression vectors capable of expression in gram-negative bacteria; and a step of preparing a polynucleotide library, wherein each expression vector contains a plurality of polypeptides having a scaffold, and the amino acid sequences of regions involved in interaction in each polypeptide are randomized, each polynucleotide among a plurality of polynucleotides encoding each of the plurality of polypeptides is inserted, a secretory signal sequence is upstream of each polynucleotide, and a polynucleotide encoding a target protein is in tandem; (b) expressing each of the expression vectors constituting the polynucleotide library in a transformed gram-negative bacterium; wherein the target protein is expressed on the inner membrane surface and the polypeptide encoded by each polynucleotide is expressed in the periplasmic space; (c) expressing each polypeptide in the periplasmic space to the target; (d) forming spheroplasts of said transformed gram-negative bacterium to select for polypeptides that bound said target protein; (e) expressing said selected polypeptides; amplifying the polynucleotide in the transformed cell to determine the amino acid sequence of the polypeptide encoded by the polynucleotide (interpreted as the method of claim 1 including providing a polynucleotide library, a plurality of expression vectors encoding a polypeptide, transforming a gram-negative bacterium with the expression vector, contacting the polypeptide with the target protein in the periplasmic space, forming a spheroplast, and identifying the polypeptide that acts on the target protein (pg. 1, claim 1). Kubo teaches that the library can display the target protein on the inner membrane surface of E.coli, and the library using the ICK scaffold has a relatively small molecular weight and high stability, so the screening process within the perismic space is also possible, wherein it was also demonstrated that the screening technique can be used to molecularly evolve a polypeptide sequence that has a higher affinity for the target membrane protein (interpreting the gram-negative bacterium; and a target membrane protein; and identifying a polypeptide that acts on the target protein based on a measured activity such as affinity, claim 1) (paragraph [0007], lines 129-133). Kubo teaches that various signal transduction that occurs via membrane proteins, such as changes in intracellular calcium, cAMP, and arachidonic acid concentrations, and changes in electrical potential, are measured using sensitive fluorescent dyes; or alternatively, an artificial lipid membrane reconstitution system containing target membrane proteins is immobilized on a substrate, and the interaction between it and polypeptides is measured using devices such as surface plasmon resonance (SPR) and quartz crystal oscillation microbalance (QCM) (interpreted as a patch clamp technique, claim 1) (paragraph [0028], lines 689-694).
Regarding claim 2, Kubo teaches that the library can display the target protein on the inner membrane surface of E.coli, and the library using the ICK scaffold has a relatively small molecular weight and high stability, so the screening process within the perismic space is also possible, wherein it was also demonstrated that the screening technique can be used to molecularly evolve a polypeptide sequence that has a higher affinity for the target membrane protein (interpreting the gram-negative bacterium to be E. coli, claim 2) (paragraph [0007], lines 129-133).
Regarding claim 3 (in part), Kubo teaches a high-throughput screening technology that is also effective in searching for ligands for membrane proteins (interpreted as membrane protein ligands, claim 3) (paragraph [0007], lines 134-135). Kubo teaches that it has been reported from mass spectrometry and steric structure analysis that this polypeptide forms three disulfide bonds and has a physicochemically and biologically stable structure (interpreted as a 3-dimensional structure; and analysis, claim 3) (paragraph [0007], lines 98-100). Kubo teaches that the tertiary structure of A4-1 was predicted using 3D modeling software components of BioPackage, and the residues involved in loop and b-sheet formation were identified by a known hynantoxin (HnTx4) (Figure 3) (interpreting BioPackage as an ODA analysis to a 3-dimensional structure analysis of a ligand for a known protein, claim 3) (paragraph [0013], lines 357-359; and Figure 3). Kubo teaches that in the polypeptide library of the present invention, the amino acid sequences of the loop I, II and III regions and part of the tail region of the ICK scaffold are randomized and have affinity with the target protein; and are used for screening high polypeptides (interpreted as randomized predicted site in the amino acid sequence of the ligand, claim 3) (paragraph [0014], lines 372-374). Kubo teaches that in a randomized polypeptide, all possible amino acid residues at a given position can be present with equal or unequal probability, and only two or more of the particular amino acid residues selected for a given position can be present (interpreted as randomized polypeptides, claim 3) (paragraph [0014], lines 390-392). Kubo teaches that Figure 1 shows the regions predicted to form loops and the amino acid residues around them were randomized (interpreted as preparing polypeptide in which the predicted site is randomized; and forming a polypeptide library, claim 3) (paragraph [0031], lines 751-752; and Figure 1).
Regarding claim 4, Kubo teaches that the polypeptide comprises the amino acid sequence of any one of SEQ ID NOS: 3 to 14, which has a high affinity for the m2 receptor (interpreting the m2 receptor as a membrane receptor, claim 4) (paragraph [0008], lines 276-277). Kubo teaches that as the target protein, not only calcium channels, which are the original target, but also various ion channels, receptors, enzymes, and other natural and non-natural compounds can be selected as targets (interpreted as including ion channel and receptors as target proteins, claim 4) (paragraph [0014], lines 375-377).
Regarding claim 6, Kubo teaches that it is possible to produce a second polypeptide library consisting of a group of a plurality of polypeptides, some of which are identical in amino acid sequence to those of the polypeptides selected in the previous round and differ in the remaining amino acids, wherein this second polypeptide library can then be used to select polypeptides that bind the target, followed by multiple rounds of selection and further randomization of the library, and so on, such that it becomes possible to introduce further mutations into the target-binding polypeptides to promote artificial molecular evolution; and that each round, amplification, transformation (or transcription/translation), and selection are sequentially repeated, such that after repeating selection/concentration for 5 or more rounds, peptide sequences converge into about 10 groups (interpreted as concentrating the polypeptide library for the first polynucleotide encoding a polypeptide that binds to a target protein prior to performing the method, claim 6) (paragraph [0025], lines 624-630 and 639-641).
Kubo does not specifically exemplify a patch-clamp technique configured to measure current flow (claim 1, in part); and applying optimal docking area (ODA) (claim 3, in part).
Regarding claim 1, Kimura teaches that it is thought that the expression of membrane proteins on E. coli inner membranes is difficult; and since only a small quantity of membrane protein can be expressed on E. coli inner membranes, techniques for the direct measurement of the activity of the expressed membrane proteins on the E. coli inner membrane have been developed to allow the observation of the expression of small protein quantities that could not otherwise be detected, such that when the E. coli cells are proliferating, inhibition of cell division by antibiotics results in long, rod-shaped E. coli, called “snake” (interpreted as expressed in E. coli; inner membrane; a membrane protein; interpreting inhibition by antibiotics as an antagonist, claim 1) (pg. 264, col 2, fifth full paragraph, lines 1-10). Kimura teaches that by removing the outer membrane of these snake bacteria through techniques such as enzymatic treatment, giant spheroplasts with diameters of over 5 μm can be obtained, such that through the application of patch-clamp electrophysiological techniques to these giant spheroplasts, the activity of ion channels expressed in the E. coli inner membrane can be directly measured, wherein successful measurement of expression using the patch clamp technique serves to confirm expression of the target ion channel on E. coli inner membranes, such that in ion channels, some GPCRs are expressed on E. coli inner membranes; and as detailed, human type 2 muscarinic acetylcholine receptor has been used for the PERISS technique (interpreted as removing a portion of the cell wall; and a patch-clamp technique to measure antagonist or agonist activity, claim 1) (pg. 264, col 2, fifth full paragraph, lines 10-20). Kimura teaches that if the target molecule is a soluble protein, it will diffuse into the E. coli periplasmic space if it is expressed in the periplasm; however, the target molecule needs to be immobilized in the E. coli inner membrane for the PERISS screening technique, such that by immobilizing a soluble protein on the E. coli inner membrane as a membrane protein, it can then be treated as a target molecule, wherein methods for immobilizing soluble proteins on the E. coli inner membrane that are similar to the APEx techniques are described in Section E. coli periplasm peptide display techniques; however, instead of using these methods, a method is developing, wherein the soluble protein is fused onto the side of a membrane protein facing the periplasmic space; and with this technique, either membrane proteins or soluble proteins can be used as target molecules for the PERISS technique (pg. 264, col 2, last partial paragraph; and pg. 265, col 1, first partial paragraph). Figure 1 is shown below:
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Kimura teaches in Figure 1, a summary of the PERISS technique including: Step (1): the target molecule and library peptide are inserted into a plasmid in tandem; Step (2): this plasmid is inserted into E. coli., the target molecule is expressed on the E. coli inner membrane, and the peptide library is expressed in the periplasmic space; Step. (3): the E. coli outer membrane is removed and peptides that did not bind to the target molecule are washed away, wherein the peptides that bound to the target molecule are collected by magnetic beads; Step (4): a portion of the peptide library on the plasmids in the E. coli is amplified by PCR, and once again integrated into plasmids, then Steps 1-4 are repeated, and ultimately the amino acid sequence of a peptide that binds to the target molecule can be determined by analyzing the DNA sequence of the peptide library in the plasmids (interpreted as preparing the polynucleotide library; and repeatedly selecting and amplifying the first polynucleotides encoding polypeptides that bind to the target protein, claims 3 and 6) (pg. 266, Figure 1).
Although the combined references of Kubo and Kimura do not specifically exemplify applying optimal docking area (ODA), Kubo does teach polypeptide libraries that can be used as a high-throughput screening system for agonists and antagonists that target membrane proteins, and identifying peptide-protein interactions, and identifying polypeptides that bind a selected protein; and Kimura does teach peptide display techniques, and screening techniques using the periplasmic expression of peptide libraries for binding against target membrane proteins, wherein it is known that Optimal Docking Area (ODA) can be used for the 3D molecular modeling of toxins using colored spheres to indicate optimal docking areas at surface points around ribbon structure of toxins, wherein secondary and tertiary structure prediction in silico revealed that motif peptides GTx1-15 and PaurTx3 from spider venom show very similar b-strand composition and distribution of optimal docking areas; and that ODA can be used to predict protein-protein interactions; as well as, successfully predict protein-protein interface regions based on sphere distribution as evidenced by Kimura and Kubo (Abstract; pg. 9, last partial paragraph; pg. 10, third full paragraph, lines 10-12; and pg. 11, Figure 2), such that one of ordinary skill in the art would clearly recognize that ODA can be applied to assess 3D molecular modeling of toxins for binding against a selected membrane protein including to measuring electrostatic potential, to identify ligand binding residues, identify optimal docking areas, and determine optimal desolvation areas to predict peptide-protein interactions and docking regions on docking partner proteins.
“It is prima facie obvious to combine prior art elements according to known methods to yield predictable results; the court held that, "…a conclusion that a claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would have yielded nothing more than predictable results to one of ordinary skill in the art. KSR International Co. v. Teleflex Inc., 550 U.S. ___, ___, 82 USPQ2d 1385, 1395 (2007); Sakraida v. AG Pro, Inc., 425 U.S. 273, 282, 189 USPQ 449, 453 (1976); Anderson’s-Black Rock, Inc. v. Pavement Salvage Co., 396 U.S. 57, 62-63, 163 USPQ 673, 675 (1969); Great Atlantic & P. Tea Co. v. Supermarket Equipment Corp., 340 U.S. 147, 152, 87 USPQ 303, 306 (1950)”. Therefore, in view of the benefits of identifying peptides that bind to selected membrane proteins for the development of new drugs and/or in identifying new drug targets as exemplified by Kimura, 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 method for creating combinatorial polypeptide libraries for identifying and screening polypeptides with high binding affinity for a desired target protein as exemplified by Kubo to include the intra-periplasm secretion and selection (PERISS) technique including methods for screening peptide libraries for activity against expressed membrane proteins as disclosed by Kimura with a reasonable expectation of success in producing a high-throughput, cost-effective method for screening polypeptide libraries for agonists and/or antagonists of membrane proteins; and/or in identifying peptides having a strong binding affinity to a selected target protein in order to identify ligands for membrane proteins.
Thus, in view of the foregoing, the claimed invention, as a whole, would have been obvious to one of ordinary skill in the art at the time the invention was made. Therefore, the claims are properly rejected under 35 USC §103 as obvious over the art.
Conclusion
Claims 1-4 and 6 are rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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 AMY M BUNKER whose telephone number is (313) 446-4833. The examiner can normally be reached on Monday-Friday (6am-2:30pm).
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/AMY M BUNKER/
Primary Examiner, Art Unit 1684
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