DETAILED ACTION 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. Priority Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Information Disclosure Statement The information disclosure statement (IDS) was submitted on 10/12/2023 before the mailing of a first office action. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Nucleotide and/or Amino Acid Sequence Disclosures Summary of Requirements for Patent Applications Filed O n Or After July 1, 2022, T hat Have Sequence Disclosures 37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted: 1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying: a. the name of the XML file b. the date of creation; and c. the size of the XML file in bytes; or 2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying: a. the name of the XML file; b. the date of creation; and c. the size of the XML file in bytes. SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS: Specific deficiency - This application fails to comply with the requirements of 37 CFR 1.831-1.834 because it does not contain a “Sequence Listing XML” as a separate part of the disclosure. A “Sequence Listing XML” is required because 1.831(b)(1) states: “ An unbranched sequence or linear region of a branched sequence containing 4 or more specifically defined amino acids, wherein the amino acids form a single peptide backbone .” The specification recites unbranched sequences of 4 or more specifically defined amino acids on page 4, lines 3, 5, 8, 11; page 10, Table 1; page 14, lines 1, 4, 7, 10 . Required response - Applicant must provide: • A “Sequence Listing XML” part of the disclosure, as described above in item 1. or 2.; together with o A statement that indicates the basis for the amendment , with specific references to particular parts of the application as originally filed, as required by 37 CFR 1.835(a)(3); o A statement that the “Sequence Listing XML” includes no new matter as required by 37 CFR 1.835(a)(4) AND • A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation by reference paragraph as required by 37 CFR 1.835(a)(2), consisting of: o A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version); o A copy of the amended specification without markings (clean version); and o A statement that the substitute specification contains no new matter. Specific deficiency - Sequences appearing in the specification are not identified by sequence identifiers (i.e., “SEQ ID NO:X” or the like) in accordance with 37 CFR 1.831(c). The specification recites unbranched sequences of 4 or more specifically defined amino acids on page 4, lines 3, 5, 8, 11; page 10, Table 1; page 14, lines 1, 4, 7, 10. Claim 2 also recites unbranched sequences of 4 or more specifically defined amino acids. Required response – Applicant must provide: A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers, consisting of: • A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version); • A copy of the amended specification without markings (clean version); and • A statement that the substitute specification contains no new matter. Claim Status Claims 1-11, filed 10/12/2023, are pending. Claims 1-11 are under examination. Specification The disclosure is objected to because of the following informalities. The specification recites unbranched sequences of 4 or more specifically defined amino acids on page 4, lines 3, 5, 8, 11; page 10, Table 1; page 14, lines 1, 4, 7, 10 that lack sequence identifiers. Appropriate correction is required. Claim Objections Claim 2 is objected to because of the following informalities. Claim 2 recites sequences that require the presence of SEQ ID NOs but lack SEQ ID NOs. Appropriate correction is required. Claims 3-8 are objected to because they depend from claim 2 and do not include sequence identifiers. Claim 9 is objected to because of the following informalities. Claim 9 recites the phrase “ bromoacetylate peptoids ” in line 6. This is better written as “ bromoacetylated peptoids ”. This is the more common way to write this. Appropriate correction is required. 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 appl icant regards as his invention. Claims 2-8 and 10 -11 are 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 the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Regarding claim 2, claim 2 recites ” The antimicrobial peptoid of claim 1, which is at least one selected from those represented by Formulas 2 to 5 below: …”. The phrase “at least one” implies that is would be possible to select more than one formula from the list. It is not clear how such a selection would be possible. Claim 2 is rejected. Regarding claim 3, claim 3 recites “An antimicrobial comprising at least one of the antimicrobial peptoids , selected in claim 2, as an active ingredient. ” This claim does not resolve the indefiniteness of claim 2 with respect to selecting more than one mutually exclusive formula. Claim 3 is rejected. Regarding claim 4, claim 4 recites The composition of claim 3, wherein the antimicrobial peptoid exhibits antimicrobial activity against gram-positive bacteria or gram-negative bacteria. First, claim 3 recites “an antimicrobial composition” and claim 4 recites “the composition”, so a lack of antecedent basis exists. Second, it is not entirely clear to which peptoid claim 4 is referring to. Claim 3 refers to peptoids in plural form, but claim 2 refers to the antimicrobial peptoid of claim 1 in the singular. So does this claim refer to all peptoids of claim 2? Clarification is requested. Finally, claim 4 does not resolve the indefiniteness of claim 3. Claim 4 is rejected. Regarding claims 5-8, these claims do not resolve the indefiniteness of claim 4. Therefore, claims 5-8 are rejected. Regarding claim 10, claim 10 recites “performing a counter ion substitution reaction by removing trifluoroacetate (TFA)…” Claim 9 does not require or recite trifluoroacetate (TFA). Therefore, this is a lack of antecedent basis and additionally it is not clear how TFA is removed when it was never added in the first place. Claim 10 is rejected. Regarding claim 11, claim 11 does not resolve the indefiniteness of claim 10. Claim 11 is rejected. The following is a quotation of the first paragraph 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 the first paragraph of pre-AIA 35 U.S.C. 112: 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. Claim 1 is 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. Claim 1 recites a formula that yields 6^12 = 2.18 X 10^9 possible peptide combinations. This is a very large genus and claim 1 requires antimicrobial activity. In this case, 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, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or 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 the inventor was in possession of the claimed genus. See Eli Lilly , 119 F.3d at 1568, 43 USPQ2d at 1406. (MPEP § 2163 (II.A.3.a.ii.)) According to MPEP § 2163 (II.A.3.a.ii.), a "representative number of species" means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc. , 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). As described above, claim 1 recites an extremely large genus of peptides. MPEP § 2163 (II.A.3.a.ii.) states that “for inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly , 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’” Even when several species are disclosed, these are not necessarily representative of the entire genus . AbbVie Deutschland GMBH v. Janssen Biotech , 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, as here, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. Since each genus recited in the instant claims is large, it would be very challenging to describe sufficient species to cover the structures of the entire genus. Applicant discloses 66 peptoids and reduces all of them to practice. At the time the invention was made, the level of skill for preparing peptides / peptoids with desired functional properties was high. However, even if a synthesis and selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify peptides / peptoids that yield polypeptides with the recited properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co. , 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs ., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”) Absent the conserved structure (length) provided by the provided species, the skilled artisan generally would not be able to visualize or otherwise predict, a priori , what peptide with a particular set of properties would look like structurally. Applicant discloses 66 examples and reduces those examples to practice. This is a tiny fraction of the claimed sequences, however. Therefore, t he provided examples only represent a limited structural diversity. Since only a limited number of species of peptides are taught within the claimed genus above, the instant claim above fails the written description requirement. A representative number of species has not been taught to describe this genus. Regarding the peptides, a single point mutation can change the biophysical properties of a peptide: “In summary, we have shown that the structural changes in the fibrillar state of the Aβ42 peptide that are observed to occur upon introduction of single point mutations can be accompanied by changes in the dominance of the microscopic processes by which these aggregates are themselves formed.” (Bolognesi et al. ACS Chem Bio 9:2 (2013) page 381 col. 2 para. 3) and “In summary, while ovispirin-1 and novispirin G-10 both had solution structures that were helical and amphipathic in the presence of TFE, a relatively simple change in their primary structure (a single glycine–isoleucine exchange) had profound effects on their respective toxicities for human erythrocytes and epithelial cells.” (Sawai et al. Protein Eng . 15:3 (2002) page 232 col. 1 para. 3). Furthermore, many sequences allowed by the current scope of the claims, result in non-functional aggregates. Wang (Wang, et al. MAbs . Vol. 1. No. 3. Taylor & Francis, (2009)) discloses a variety of aggregation prone motifs that occur in commercial antibodies (Wang, page 262, Table 2). The scope of the claims currently may incorporate such motifs and result in non-functional aggregates. Given this unpredictability of protein / peptoid design, the skilled artisan would not have been in possession of the substantial repertoire of peptide species encompassed by the claimed invention; one of skill in the art would conclude that applicant was not in possession of the structural attributes of a representative number of species possessed by the members of the genus of every polynucleotide molecule recited by claim 1 . Claim 1 is rejected. Examiner Note: Claim 2 remedies the written description issues of claim 1. Therefore, claim 2 and its dependent claims are not rejected for written description issues. Claim s 4 -8 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 exhibiting antimicrobial activity against E. coli and S. aureus , does not reasonably provide enablement for any possible gram-positive and gram-negative bacteria FILLIN "Identify aspects of claims for which the specification is not enabling" \* MERGEFORMAT . The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. In order to determine compliance with the enablement requirement of 35 U.S.C. 112(a), the Federal Circuit developed a framework of factors in In re Wands , 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988), referred to as the Wands factors to assess whether any necessary experimentation required by the specification is "reasonable" or is "undue." Consistent with Amgen Inc. et al. v. Sanofi et al., 598 U.S. 594, 2023 USPQ2d 602 (2023), the Wands factors continue to provide a framework for assessing enablement in a utility application or patent, regardless of technology area. Guidelines for Assessing Enablement in Utility Applications and Patents in View of the Supreme Court Decision in Amgen Inc. et al. v. Sanofi et al., 89 FR 1563 (January 10, 2024). These factors include, but are not limited to: The breadth of the claims; The breadth of claim 4 encompasses all possible gram-positive and gram-negative bacteria. The nature of the invention; The invention is an antimicrobial peptoid that exhibits activity against gram-positive and gram-negative bacteria. The state of the prior art; Chongsiriwatna et al. ( Chongsiriwatana , et al. Proceedings of the National Academy of Sciences 105.8: 2794-2799. (2008) ) discloses that peptoids are comparable in activity to AMPs: “Previous work has shown that peptoids can be used to create compounds with antimicrobial activities similar to AMPs (34). In this study, we exploited the facile synthesis and high propensity for helix formation of certain peptoids to create and study a library of ampetoid variants that suggests strong functional and mechanistic analogy between ampetoids and AMPs and that demonstrates the ampetoids ’ potential for development into clinically useful antibiotics.” Mercer et al. ( Mercer, Derry K., et al. "Antimicrobial susceptibility testing of antimicrobial peptides to better predict efficacy." Frontiers in cellular and infection microbiology 10: 326. (2020) ) discloses that the antimicrobial activity of antimicrobial peptides can be very specific:” In vivo studies in animals have demonstrated that AMP provide protection against microbial infection and that their absence results in an increased risk of infectious disease (Rivas-Santiago et al., 2009 ). In some cases, protection against infection is relatively generalised , i.e. effected by a number of AMP, such as the combination of drosomycin and metchnikowin and defence against Candida albicans infection in Drosophila melanogaster ( Imler and Bulet , 2005 ; Hanson et al., 2019 ), whereas in others interactions are very specific, e.g., diptericin and defence against Providencia rettgeri infection in D. melanogaster (Hanson et al., 2019 ) .” Lazzaro et al. ( Lazzaro, Brian P., Michael Zasloff, and Jens Rolff . "Antimicrobial peptides: Application informed by evolution." Science 368.6490: eaau5480. (2020) ) also discloses that AMPs may have specific activity: “ The previously widespread belief that AMPs have generic, broad-spectrum activity has been recently challenged by new data. For example, in vivo disruption of individual AMP genes in the beetle Tenebrio molitor causes differential sensitivity to infection by the bacterium Staphylococcus aureus ( 29 ). In Drosophila melanogaster and its sister species Drosophila simulans , naturally occurring null alleles of the AMP gene Diptericin A cause acute sensitivity to infection by the bacterium Providencia rettgeri but not to other bacteria, including close relatives of P. rettgeri (Fig. 2) ( 30 ). Furthermore, a single polymorphic amino acid substitution in the Diptericin A peptide is sufficient to specifically alter resistance to P. rettgeri , and this susceptible mutation has arisen at least five independent times across the genus Drosophila ( 31 ). These findings suggest a previously unsuspected specificity in AMP activity. ” (D) The level of one of ordinary skill; A person of ordinary skill in the art in the field of peptoid design is usually at least a Master’s level education. (E) The level of predictability in the art; Protein-protein or protein- peptoid interactions are generally unpredictable. A single point mutation can change the biophysical properties of a peptide: “In summary, we have shown that the structural changes in the fibrillar state of the Aβ42 peptide that are observed to occur upon introduction of single point mutations can be accompanied by changes in the dominance of the microscopic processes by which these aggregates are themselves formed.” (Bolognesi et al. ACS Chem Bio 9:2 (2013) page 381 col. 2 para. 3) and “In summary, while ovispirin-1 and novispirin G-10 both had solution structures that were helical and amphipathic in the presence of TFE, a relatively simple change in their primary structure (a single glycine–isoleucine exchange) had profound effects on their respective toxicities for human erythrocytes and epithelial cells.” (Sawai et al. Protein Eng . 15:3 (2002) page 232 col. 1 para. 3). Furthermore, many sequences allowed by the current scope of the claims, result in non-functional aggregates. Wang (Wang, et al. MAbs . Vol. 1. No. 3. Taylor & Francis, (2009)) discloses a variety of aggregation prone motifs that occur in commercial antibodies (Wang et al. , page 262, Table 2). The scope of the claims currently may incorporate such motifs and result in non-functional aggregates. (F) The amount of direction provided by the inventor and the existence of working examples and t he quantity of experimentation needed to make or use the invention based on the content of the disclosure. Applicant provides 66 examples reduced to practice tested against E. coli and S. aureus bacteria. Regarding claim 4, claim 4 recites t he composition of claim 3, wherein the antimicrobial peptoid exhibits antimicrobial activity against gram-positive bacteria or gram-negative bacteria. As described above, peptoids are comparable to antimicrobial peptides in terms of activity. Mercer and Lazzaro disclose that AMPs can have specific activity and therefore it is reasonable to conclude that the same is true of peptoids . Consequently, it would require undue experimentation to test the claimed peptoids against all possible bacteria strain s to ensure efficacy. Claim 4 is rejected. Regarding claim 5, claim 4 is rejected as described above. Claim 5 reduces the number of claimed bacteria, but no data is presented for these bacteria species. Consequently, it would require undue experimentation to test the claimed peptoids against the claimed bacteria strains to ensure efficacy. Claim 5 is rejected. Regarding claim 6, claim 4 is rejected as described above. Claim 6 reduces the number of claimed bacteria, but data is presented for only S. Aureus . Consequently, it would require undue experimentation to test the claimed peptoids against the claimed bacteria strains to ensure efficacy. Claim 6 is rejected. Regarding claim 7, claim 4 is rejected as described above. Claim 7 reduces the number of claimed bacteria, but no data is presented for these bacteria species. Consequently, it would require undue experimentation to test the claimed peptoids against the claimed bacteria strains to ensure efficacy. Claim 7 is rejected. Regarding claim 8, claim 4 is rejected as described above. Claim 8 reduces the number of claimed bacteria, but data is presented for only E. Coli . Consequently, it would require undue experimentation to test the claimed peptoids against the claimed bacteria strains to ensure efficacy. Claim 8 is rejected. 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. Claim 1 is rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Seo et al. KR 20190110061 , published 9/27/2019 . Regarding claim 1, claim 1 recites An antimicrobial peptoid represented by Formula 1 below: [Formula 1] H-X ₁ -Y ₁ -Z ₁ -X ₂ -Y2-Z ₂ -X ₃ -Y3-Za-X4-Y4-Z4-NH ₂ wherein X ₁ to Z ₁ , X ₂ to Z ₂ , X ₃ to Z ₃ , and X ₄ to Z ₄ are each independently Nspe , MLys , NhTrp , NHis , Npm , or N4hb. Seo et al. discloses the following peptoid : H- Nlys - Npm-Npm-Nlys-Nspe-Npm - ( Nlys-Npm-Npm ) 2-NH2 (Seo et al., page 3, line 1). In this case. X 1 is NLys , Y 1 is Npm , Z 1 is Npm , X 2 is Nlys , Y 2 is Nspe , Z 2 is Npm , X 3 is Nlys , Y 3 is Npm , Z 3 is Npm , X 4 is Nlys , Y 3 is Npm , and Z 4 is Npm . Consequently, claim 1 is anticipated by Seo et al. and rejected. 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 . Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over Molchanova, et al. ( Molchanova, et al. Molecules 22.9: 1430 (2017) ) in view of Zuckermann et al. ( Zuckermann , et al. Journal of the American Chemical Society 114.26: 10646-10647 (1992) ) . Regarding claim 9, claim 9 recites a method of preparing an antimicrobial composition, comprising: preparing deprotected polymer resin beads (S100); preparing a bromoacetylate peptoid by adding the deprotected polymer resin beads, bromoacetic acid, diisopropylcarbodiimide (DIC), and an organic solvent and performing a bromoacetylation reaction (S200); adding a submonomer to the bromoacetylate peptoids and performing an amine substitution reaction (S300); obtaining an antimicrobial peptoid having the desired sequence by repeating S200 to S300 (S400); and separating a polymer resin from the antimicrobial peptoid using a cleavage solution (S500), wherein the submonomer is at least one selected from N spe , N Lys , N hTrp , N His , N pm , and N 4hb. Molchanova discloses that antimicrobial peptoids may be synthesized using the scheme of Zuckermann : “ The focus of this review is to highlight the developments in the last decade regarding the synthesis, discovery and potential applications of antimicrobial peptidomimetics ( Figure 1 ) comprising the classes of α- peptoids ( N -alkylated glycine oligomers), β- peptoids ( N -alkylated β-alanine oligomers), β 3 -peptides, α/β 3 -peptides, α-peptide/β- peptoid hybrids, α/γ N -acylated N - aminoethylpeptides ( AApeptides ) and oligoacyllysines (OAKs). ” (Molchanova et al., page 11, para. 4). “ However, the monomer strategy is laborious and time-consuming when several different building blocks are required. Shortly after, the submonomer approach was introduced by Zuckerman et al. [ 164 ], thereby avoiding the need for synthesis of protected building blocks ( Scheme 1 C). Here, peptoid synthesis is achieved entirely by solid-phase steps: bromoacetic acid is activated with N , N - diisopropylcarbodiimide (DIC) and then reacted with a resin-bound amine in DMF; subsequent nucleophilic displacement with a primary amine gives the desired peptoid residue. This activation/substitution cycle is repeated until the target sequence is obtained. Finally, the peptoid is cleaved from the resin by using TFA. ” (Molchanova et al., page 13, para. 1) Zuckermann discloses the following method steps for the preparation of peptoids : “ Oligomer syntheses were performed on a robotic synthesizer. The syntheses were conducted with Rink amide polystyrene resin (50 Mmol, substitution level 0.45 mmol/g) to avoid diketopiperazine formation. ” ( Zuckermann et al., page 10646, col. 2, Footnote). ( preparing deprotected polymer resin beads (S100) ) “ Acylation reactions were performed by addition of bromoacetic acid (600 Mmol, 83 mg) in DMF (0.83 mL), followed by addition of /V./V'- diisopropylcarbodiimide (660 Mmol, 103 pL ) in DMF (170 mL). ” ( Zuckermann et al., page 10646, col. 2, Footnote). ( preparing a bromoacetylate peptoid by adding the deprotected polymer resin beads, bromoacetic acid, diisopropylcarbodiimide (DIC), and an organic solvent and performing a bromoacetylation reaction (S200) ) “ Reaction mixtures were agitated at room temperature for 30 min. Each acylation was repeated once. Displacement reactions were performed by addition of primary amine (2.0 mmol) as 2.5 M solutions in dimethyl sulfoxide (1.0 mL), followed by agitation for 2 h at room temperature. ” ( Zuckermann et al., page 10646, col. 2, Footnote) ( performing an amine substitution reaction (S300); “ Here, peptoid synthesis is achieved entirely by solid-phase steps ” (Molchanova et al., page 13, para. 1) ( obtaining an antimicrobial peptoid having the desired sequence by repeating S200 to S300 (S400) ) Optimization of displacement reactions was performed by varying amine concentrations from 0.25 to 2.5 M. Side-chain protecting groups were removed, and the oligomer was released from the resin support by treatment of the oligomer-resin with 95% trifluoroacetic acid in water (10 mL) for 20 min at room temperature, followed by filtration, dilution, and lyophilization. ” ( Zuckermann et al., page 10646, col. 2, Footnote). ( separating a polymer resin from the antimicrobial peptoid using a cleavage solution (S500) ) Zuckermann discloses that peptoids may include NLys or Npm . ( Zuckermann et al., page 10647, Table 1). It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to use the specific process disclosed by Zuckermann to create the antimicrobial peptoid disclosed by Molchanova. A person of ordinary skill in the art would be motivated to make this combination because Molchanova specifically lists this method as an effective way of synthesizing antimicrobial peptoids and have a reasonable expectation of success because Molchanova discloses that this method is regularly used for this purpose (Molchanova et al., page 13, Scheme 1). Consequently, claim 9 is obvious over Molchanova et al. in view of Zuckermann et al. and rejected. Claim s 10 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Molchanova, et al. ( Molchanova, et al. Molecules 22.9: 1430 (2017) ) in view of Zuckermann et al. ( Zuckermann , et al. Journal of the American Chemical Society 114.26: 10646-10647 (1992) ) as applied to claim 9 above, further in view of Roux et al. ( Roux, et al. Journal of peptide science: an official publication of the European Peptide Society 14.3: 354-359 (2008) ) as evidenced by Crystal Quest ( https://crystalquest.com/blogs/ion-exchange/anion-exchange-resin , accessed 3/17/2026). Regarding claim 10, claim 9 is obvious as described above. Claim 10 further compris es , after S500, performing a counter ion substitution reaction by removing trifluoroacetate (TFA) ions included in the composition using a carbonate ion exchange resin and adding an acidic solution (S600). Loux discloses the process of such an ion exchange: “ To conduct the exchange from TF-acetate to acetate, a strong anion resin was chosen (AG1-X8, quaternary ammonium). In order to ensure a total counter ion exchange, a high excess of 245 mg of this resin was prepared as follows: the resin was successively washed three times with 1.6 N acetic acid (10 ml) and three times with 0.16 N acetic acid (10 ml). The peptide solution (19.9 mg in 4 ml of water) was then poured on the resin. After 1 h of rotary stirring, the peptide-resin suspension was filtered and the liquid phase recovered. The resin was washed twice with 1 ml of water, the solutions were pooled and the peptide was isolated after freeze-drying. The pH was monitored during the process. The initial pH of the peptide TFA salt in pure water was 6.5, and the pH of the resin beads in 4 ml of pure water was 3.1, which can be considered as a mild pH. ” ( Loux et al., page 355, col. 2, para. 2). Crystal Quest discloses that carbonate ions are target of anion exchange columns as disclosed by Loux (Crystal Quest, page 5, bottom table). It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to add the step disclosed by Loux to the method of Molchanova and Zuckermann to arrive at the claimed invention. A person would be motivated to use the extra step of Loux because Loux discloses that the residual trifluoroacetate ion is problematic and traditional methods of removal have downsides: “ Even though the excess TFA is easy to remove by a classic freeze-drying method, it is more challenging to remove the TF-acetate counter-ion, which strongly interacts with the positive charges of cationic peptides. Hitherto, the most convenient procedure to replace the TF-acetate counter-ion by another counter-ion has been mixing the peptide with an excess of a stronger acid than TFA, followed by a freeze-drying step [12]. A stronger acid than TFA is able to reprotonate the TF-acetate into its free acid form, which is then easily removed by freeze-drying [13]. However, this approach has essentially two drawbacks: ( i ) the very acidic solution can chemically damage the peptides, and (ii) the very restrictive choice of possible counterions, i.e. the counter-ions that are associated with strong acids (e.g. HCl, H2SO4, HF, HNO3). ” ( Loux et al., page 354, col. 2, para. 3). A person of ordinary skill in the art would have a reasonable expectation of success because Loux describes this process as successful: “ We have described two fast, efficient and reproducible protocols to remove TF-acetate counter-ions. These two methods were monitored by both 19F-NMR and 1H-NMR spectroscopy. More than 95% TF-acetate counter-ions were exchanged with acetate counter-ion. ” ( Loux et al., page 359, col. 1, para. 3). Consequently, claim 10 is obvious over Molchanova et al. in view of Zuckermann et al. as applied to claim 9 above, further in view of Loux et al. as evidenced by Crystal Quest and rejected. Regarding claim 11, claim 10 is obvious as described above. Loux discloses the usage of acetic acid in their process: : “ To conduct the exchange from TF-acetate to acetate, a strong anion resin was chosen (AG1-X8, quaternary ammonium). In order to ensure a total counter ion exchange, a high excess of 245 mg of this resin was prepared as follows: the resin was successively washed three times with 1.6 N acetic acid (10 ml) and three times with 0.16 N acetic acid (10 ml). The peptide solution (19.9 mg in 4 ml of water) was then poured on the resin. After 1 h of rotary stirring, the peptide-resin suspension was filtered and the liquid phase recovered. The resin was washed twice with 1 ml of water, the solutions were pooled and the peptide was isolated after freeze-drying. The pH was monitored during the process. The initial pH of the peptide TFA salt in pure water was 6.5, and the pH of the resin beads in 4 ml of pure water was 3.1, which can be considered as a mild pH. ” ( Loux et al., page 355, col. 2, para. 2). Consequently, claim 11 is obvious over Molchanova et al. in view of Zuckermann et al. as applied to claim 9 above, further in view of Loux et al. as evidenced by Crystal Quest and rejected. 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 . Claim 1 is rejected on the ground of nonstatutory double patenting a s being unpatentable over claim 1 of U.S. Patent No. 10,815,275 . Although the claims at issue are not identical, they are not patentably distinct from each other . Regarding claim 1, claim 1 recites An antimicrobial peptoid represented by Formula 1 below: [Formula 1] H-X ₁ -Y ₁ -Z ₁ -X ₂ -Y2-Z ₂ -X ₃ -Y3-Za-X4-Y4-Z4-NH ₂ wherein X ₁ to Z ₁ , X ₂ to Z ₂ , X ₃ to Z ₃ , and X ₄ to Z ₄ are each independently Nspe , MLys , NhTrp , NHis , Npm , or N4hb. The ‘275 patent discloses the following in claim 1: “ 1. A peptoid having any one formula selected from the following Formulae 1, 2 and 5: H- Nlys - Npm-Npm-Nlys-Nspe-Npm -( Nlys-Npm-Npm ) 2 -NH 2 ; [Formula 1] H-( Nlys-Npm-Npm ) 2 -Nlys-Nspe-Npm-Nlys-Npm-Npm-NH 2 ; and [Formula 2] H- Nlys - Npm-Npm -( Nlys-Nspe-Nspe ) 2 -Nlys-Npm-Npm-NH 2 . [Formula 5] ” Consequently, claim 1 is anticipated by the ‘275 patent and claim 1 is rejected. Closest Prior Art The sequences disclosed by claim 2 are novel and nonobvious. The closest prior art is found in Seo et al. KR 20190110061 , published 9/27/2019 . Seo discloses such peptoids as H- Nlys - Npm-Npm-Nlys-Nspe-Npm - ( Nlys-Npm-Npm ) 2-NH2 (Seo et al., page 3, line 1). However, Seo does not disclose the peptoids of claim 2, specifically the peptoids of Seo do not include NhTrp residues nor do they utilize Nlys and Nspe in the same patterns. Seo also does not reasonably teach or suggest the substitutions to achieve the peptoids of claim 2. The next closest prior art , Chongsiriwatana , et al. Proceedings of the National Academy of Sciences 105.8: 2794-2799 (2008) ), discloses a peptoid such as ( Nlys-Nspe-Nspe ) 4 ( Chongsiriwatana et al., page 2795, Table 1). However, fails to disclose usage of NhTrp , much less NhTrp in the same pattern as the present application. Claim 3 is an antimicrobial composition containing the peptoid of claim 2, so it is also free of the prior art as currently claimed. Conclusion No claim is allowed. Claims 2 -9 are objected to. Claims 1 and 4-11 are rejected. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT David Paul Bowles whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-0919 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT Monday-Friday 8:30-5:00 . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. 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For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /DAVID PAUL BOWLES/ Examiner, Art Unit 1654 /LIANKO G GARYU/ Supervisory Patent Examiner, Art Unit 1654