A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 5/19/2026 has been entered.
DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Amendment after Final office action filed on 5/19/2026 is acknowledged.
3. Claim filed on 5/19/2026 is acknowledged.
4. Claims 1-25 and 27 have been cancelled.
5. New claims 42 and 43 have been added.
6. Claims 26 and 28-43 are pending in this application.
7. Claims 40 and 41 remain withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim.
8. Applicant elected without traverse of Group 1 (claims 26-39) and elected peptide of SEQ ID NO: 109 as species of peptide; peptide of SEQ ID NO: 109 conjugated to polyethylene glycol (PEG) polymer as species of conjugate; and a composition comprising peptide of SEQ ID NO: 109 and solubilizing agent in the form of serum as species of composition in the reply filed on 3/26/2025.
Restriction requirement was deemed proper and made FINAL in the previous office actions. Group 1 is drawn to an anti-inflammatory peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-319, 320-325, and 327, and wherein the peptide is up to 50 amino acids in length; a conjugated comprising such peptide conjugated to a polyethylene glycol (PEG) polymer, a water-soluble polymer moiety, homo or co-polymers of PEG, a monomethyl-substituted polymer of PEG (mPEG) and polyoxyethylene glycerol (POG), albumin, gelatin, a fatty acid, polysaccharide, a lipid amino acid, dextran, a lipophilic group, or an antibody molecule; and a composition comprising such peptide. A search was conducted on the elected species; and these appear to be free of prior art. A search was extended to the genus in claims 26, 31 and 32; and these too appear to be free of prior art. Claims 26, 28-39, 42 and 43 are examined on the merits in this office action.
Please note: The sequence listing in computer readable format filed on 5/19/2026 is defective. Applicant is required to address this issue.
Claim Interpretations
9. With regards to the limitations recited in instant claims 29 and 30, as stated in the previous office actions, the Examiner is interpretating instant claims 29 and 30 include all the limitations of instant claim 26. Therefore, the peptide recited in instant claim 29 or 30 needs to meet the limitation “wherein the peptide is up to 50 amino acids in length” recited in instant claim 26.
Withdrawn Objections and Rejections
10. Objection to claims 31, 33 and 37 is hereby withdrawn in view of Applicant’s amendments to the claim.
11. Rejection to claim 31 under 35 U.S.C. 101 is hereby withdrawn in view of Applicant’s amendment to the claim.
12. Rejection to claim 31 under 35 U.S.C. 102(a)(1) as being anticipated by the glutelin [Oryza sativa] document (cited and enclosed in the previous office action, from https://www.ncbi.nlm.nih.gov/protein/BAA36695.1?report=genbank&log$=protalign&blast_rank=1&RID=YB9NZT7S013, 1999, pages 1-2) is hereby withdrawn in view of Applicant’s amendment to the claim.
Maintained/Revised Objections
13. Claim 28 remains objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Response to Applicant's Arguments
14. Applicant fails to address this objection. Therefore, the objection is deemed proper and is hereby maintained.
New Objections
15. Claim 26 is objected to for the following minor informality: Applicant is suggested to amend claim 26 as “An anti-inflammatory peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325 and 327; wherein the peptide is up to 50 amino acids in length”.
16. Claim 42 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
17. Claim 43 is objected to for the following minor informality: Applicant is suggested to amend the recited “SEQ ID Nos:” as “SEQ ID NOs:”.
Maintained/Revised Rejections
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
18. 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.
19. (Revised due to Applicant’s amendment to the claim) Claims 26, 29-39 and 43 remain/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 MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient” (MPEP § 2163).
A claimed genus may be satisfied through sufficient description of a representative number of species or disclosure of relevant, identifying characteristics such as functional characteristics coupled with a known or disclosed correlation between function and structure (MPEP § 2163(3)a(II)). The number of species that describe the genus must be adequate to describe the entire genus; if there is substantial variability, a large number of species must be described.
The analysis for adequate written description considers (a) actual reduction to practice, (b) disclosure of drawings or structural chemical formulas, (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure, and (d) representative number of samples.
In the instant case, claims 26, 29-39 and 43 recite an anti-inflammatory peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-319, 320-325, and 327, and wherein the peptide is up to 50 amino acids in length; a conjugated comprising such peptide conjugated to a polyethylene glycol (PEG) polymer, a water-soluble polymer moiety, homo or co-polymers of PEG, a monomethyl-substituted polymer of PEG (mPEG) and polyoxyethylene glycerol (POG), albumin, gelatin, a fatty acid, polysaccharide, a lipid amino acid, dextran, a lipophilic group, or an antibody molecule; and a composition comprising such peptide.
The genus of instant claimed peptide is very broad, including any peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325, and 327, and wherein the peptide is up to 50 amino acids in length.
The instant specification discloses the peptide of instant SEQ ID NO: 109 as an anti-inflammatory peptide that reduces the secretion of TNFα by LPS-stimulated J774.2 macrophages. Peptides of instant SEQ ID NOs: 268-284, 286-325 and 327 are variants of instant SEQ ID NO: 109 having 1 to 3 amino acid alterations.
The issue at question is whether a person of ordinary skilled in the art would be able to determine what structural feature/amino acid sequence is required for the instant claimed peptide to have the functional characteristics of being an anti-inflammatory peptide or not.
(a) actual reduction to practice and (b) disclosure of drawings or structural chemical formulas:
In the instant case, the instant specification discloses the peptide of instant SEQ ID NO: 109 as an anti-inflammatory peptide that reduces the secretion of TNFα by LPS-stimulated J774.2 macrophages.
The instant specification further discloses peptides of instant SEQ ID NOs: 268-284, 286-325 and 327 as variants of instant SEQ ID NO: 109 having 1 to 3 amino acid alterations.
In addition, peptides of instant SEQ ID NOs: 109 and 320 are tested in the working examples of instant specification. The peptide of SEQ ID NO: 320 consists of the amino acid sequence RGPQQYAEWQINE, which is a variant of the peptide of instant SEQ ID NO: 109 (consisting of the amino acid sequence RGPQQYAEWQINEK) with K at position 14 is deleted. And based on the data presented in instant specification, the peptide of instant SEQ ID NO: 320 reduces the secretion of TNFα by 13% (see Figure 7; and page 61, Table 1); and such reduction on the secretion of TNFα is significantly less than that of the peptide of instant SEQ ID NO: 109 (see SP2 in Figure 22A).
Taken all these together, other than the limited examples, the instant specification fails to disclose the effect of altering the amino acid sequence of instant SEQ ID NO: 109 on the functional characteristics of being an anti-inflammatory peptide. The instant specification does not describe a general correlation between structure and function for the claimed genus of peptide.
(c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure:
As discussed above, in the instant case, based on the disclosure of instant specification, other than the limited examples, a person of ordinary skilled in the art would not be able to determine the effect of altering the amino acid sequence of the peptide of instant SEQ ID NO: 109 on the functional characteristics of being an anti-inflammatory peptide.
With regards to the instant claimed peptide being an anti-inflammatory peptide, it is unknown in the art.
Furthermore, it is well known in the peptide/protein art that even single amino acid changes or differences in the amino acid sequence of a protein can have dramatic effects on the protein’s function. As an example of the unpredictable effects of mutations on protein function, Drumm et al (Annu. Rev. Pathol. Mech. Dis., 2012, 7, pages 267-282, filed with IDS) teach cystic fibrosis is an autosomal recessive disorder caused by mutations in the CFTR (cystic fibrosis transmembrane conductance regulator) gene, for example, page 268, Section “CYSTIC FIBROSIS”. Drumm et al further teach several mutations can cause cystic fibrosis, including two mutations G551D and G551S; and clinical consequences are quite different for these two changes, as the G551D variant has virtually no detectable activity, and consequently a classic, severe phenotype is associated; G551S, however, has reduced but clearly detectable function and is associated with a much milder presentation of CF, for example page 269, left column, the last paragraph. Drumm et al also teach that in the most common cystic fibrosis mutation ΔF508 (the absence of amino acid 508 of the normally 1,480-amino acid protein) gives rise to the cystic fibrosis phenotype, for example, page 268, right column, the 2nd paragraph. Thus, even the substitution or deletion of a single amino acid can have dramatic and unpredictable effects on the function of the protein. The unpredictability of the effect of amino acid substitution on the function and/or property of peptide/protein is further confirmed and discussed in Yampolsky et al (Genetics, 2005, 170, pages 1459-1472, filed with IDS). Yampolsky et al teach even conservative substitution can significantly affect the function of the protein/peptide, for example, page 1465, Table 3. Although the disclosures of Drumm et al and Yampolsky et al are directed to proteins/peptides other than an anti-inflammatory peptide, they illustrate the inherent unpredictability with respect to the biological activity of a given protein/peptide after even minor changes to the primary amino acid sequence.
Therefore, based on the state of art, a person of ordinary skilled in the art would not be able to determine the effect of altering the amino acid sequence of the peptide of instant SEQ ID NO: 109 on the functional characteristics of being an anti-inflammatory peptide. The instant specification does not describe a general correlation between structure and function for the claimed genus of peptide.
(d) representative number of samples:
In the instant case, the genus of instant claimed peptide is very broad, including any peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325, and 327, and wherein the peptide is up to 50 amino acids in length.
And, as discussed in (a) and (b) above, the instant specification discloses the peptide of instant SEQ ID NO: 109 as an anti-inflammatory peptide that reduces the secretion of TNFα by LPS-stimulated J774.2 macrophages.
The instant specification further discloses peptides of instant SEQ ID NOs: 268-284, 286-325 and 327 as variants of instant SEQ ID NO: 109 having 1 to 3 amino acid alterations.
In addition, peptides of instant SEQ ID NOs: 109 and 320 are tested in the working examples of instant specification. The peptide of SEQ ID NO: 320 consists of the amino acid sequence RGPQQYAEWQINE, which is a variant of the peptide of instant SEQ ID NO: 109 (consisting of the amino acid sequence RGPQQYAEWQINEK) with K at position 14 is deleted. And based on the data presented in instant specification, the peptide of instant SEQ ID NO: 320 reduces the secretion of TNFα by 13% (see Figure 7; and page 61, Table 1); and such reduction on the secretion of TNFα is significantly less than that of the peptide of instant SEQ ID NO: 109 (see SP2 in Figure 22A).
Considering the broadness of the genus of instant claimed peptide, the instant specification fails to provide sufficient examples to describe the entire genus of peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325, and 327, and wherein the peptide is up to 50 amino acids in length being an anti-inflammatory peptide claimed.
Taken all these together, considering the state of the art and the disclosure in instant specification, it is deemed that the instant specification fails to provide adequate written description for the claimed genus of peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325, and 327, and wherein the peptide is up to 50 amino acids in length being an anti-inflammatory peptide; and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Response to Applicant's Arguments
20. Applicant argues that “claim 26 is amended to recite specific peptides that are tested or closely related to the peptides tested in the working examples of the instant specification.”; and “Applicants note that in the Examiner Proposed Amendments discussed on October 21, 2024, Examiner Komatsu proposed the possibility of adding the now recited SEQ ID NOs into claim 26 or into a new claim.”
21. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, the Examiner would like to point out that as stated in Section 19 above, the instant specification discloses the peptide of instant SEQ ID NO: 109 as an anti-inflammatory peptide that reduces the secretion of TNFα by LPS-stimulated J774.2 macrophages. The instant specification further discloses peptides of instant SEQ ID NOs: 268-284, 286-325 and 327 as variants of instant SEQ ID NO: 109 having 1 to 3 amino acid alterations. However, only peptides of instant SEQ ID NOs: 109 and 320 are tested in the working examples of instant specification. The peptide of SEQ ID NO: 320 consists of the amino acid sequence RGPQQYAEWQINE, which is a variant of the peptide of instant SEQ ID NO: 109 (consisting of the amino acid sequence RGPQQYAEWQINEK) with K at position 14 is deleted. And based on the data presented in instant specification, the peptide of instant SEQ ID NO: 320 reduces the secretion of TNFα by 13%; and such reduction on the secretion of TNFα is significantly less than that of the peptide of instant SEQ ID NO: 109. Furthermore, it is well known in the peptide/protein art that even single amino acid changes or differences in the amino acid sequence of a protein can have dramatic effects on the protein’s function. Therefore, in the instant case, considering the state of the art and the disclosure in instant specification, it is deemed that the instant specification fails to provide adequate written description for the claimed genus of peptide comprising the amino acid sequence selected from the group consisting of SEQ ID NOs: 109, 268-284, 286-325, and 327, and wherein the peptide is up to 50 amino acids in length being an anti-inflammatory peptide; and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
With regards to Applicant’s arguments based on the Examiner’s proposed claim amendment discussed on 10/21/2024, the Examiner would like to point out that the proposed claim amendments do not recite the functionality/property of being an anti-inflammatory peptide.
Taken all these together, the rejection is deemed proper and is hereby maintained.
Examiner’s Notes
22. The peptide, the conjugate and the composition recited in instant claims 26, 28-39, 42 and 43 are free of prior art. The closest prior art is La Rosa et al (US 2004/0123343 A1, cited and enclosed in the previous office actions). La Rosa et al teach peptide of SEQ ID NO: 180826, which is 83 amino acids in length and comprises the amino acid sequence of instant SEQ ID NO: 109, as shown below with Qy being instant SEQ ID NO: 109 and Db being the peptide of SEQ ID NO: 180826 in La Rosa et al:
PNG
media_image1.png
184
900
media_image1.png
Greyscale
. However, there is no teaching, motivation, or other type of suggestion to modify the peptide of SEQ ID NO: 180826 in La Rosa et al and arrive at the peptide, the conjugate and the composition recited in instant claims 26, 28-39, 42 and 43. Therefore, the peptide, the conjugate and the composition recited in instant claims 26, 28-39, 42 and 43 are both novel and unobvious over the prior arts of record. And the claimed peptide, the conjugate and the composition are markedly different from what exist in nature.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LI N KOMATSU whose telephone number is (571)270-3534. The examiner can normally be reached Mon-Fri 8am-4pm EST.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658
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