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 Non-final office action filed on 11/10/2025 is acknowledged.
3. Claim filed on 11/10/2025 is acknowledged.
4. Claims 1-25 and 27 have been cancelled.
5. Claims 26 and 28-41 are pending in this application.
6. Claims 40 and 41 remain withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim.
7. 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 action. Group 1 is drawn to an anti-inflammatory peptide comprising the amino acid sequence of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length; a conjugated comprising such peptide conjugated, linked or fused to a binding partner, in which the binding partner is selected from 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), a polyamino acids, a pharmacologically inactive proteins selected from 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 the genus in claims 26 and 32 appear to be free of prior art. However, prior art was found for the genus in claim 31. Claims 26 and 28-39 are examined on the merits in this office action.
Claim Interpretations
8. With regards to the limitations recited in instant claims 29 and 30, as stated in the previous office action, 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 “comprising the amino acid sequence of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length” recited in instant claim 26.
With regards to the binding partner recited in instant claim 31, the Examiner is interpretating a molecule having the structure of any one of the Markush group recited in instant claim 31 is the binding partner recited in instant claim 31. Such interpretation applies to all the rejections set forth below.
Withdrawn Objections and Rejections
9. Objection to the specification is hereby withdrawn in view of Applicant’s amendments to the specification.
10. Objection to claims 26, 27, 29, 30, 32, 34-36, 38 and 39 is hereby withdrawn in view of Applicant’s amendments to the claim.
11. Rejection to claim 31 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph is hereby withdrawn in view of Applicant’s amendment to the claim.
12. Rejection to claim 27 under 35 U.S.C. 112(d) or 35 U.S.C. 112 (pre-AIA ), 4th paragraph is hereby withdrawn in view of Applicant’s amendment to the claim.
Maintained/Revised Objections
13. (Revised due to Applicant’s amendment to the claim) 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.
14. (Revised due to Applicant’s amendment to the claim) Claim 31 remains objected to for the following minor informality: Applicant is suggested to amend claim 31 as “A conjugate comprising the peptide of claim 26 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), a polyamino acids, albumin, gelatin, a fatty acid…”.
15. (Revised due to Applicant’s amendment to the claim) Claim 33 remains objected to for the following minor informality: Applicant is suggested to amend claim 33 as “The composition of claim 32, wherein the composition is in the form of powder”.
16. (Revised due to Applicant’s amendment to the claim) Claim 37 remains objected to for the following minor informality: Applicant is suggested to amend claim 37 as “The composition of claim 32, wherein the composition further comprises a cosmetically or pharmaceutically acceptable excipient selected from the group consisting of emollient, diluent…”.
Response to Applicant's Arguments
17. Applicant either fails to address all the minor issues in these claims or Applicant’s amendment to the claim introduces additional minor issues into these claims. Therefore, these objections are deemed proper and are hereby maintained.
Maintained/Revised Rejections
Claim Rejections - 35 U.S.C. § 101
18. 35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
19. (Revised due to Applicant’s amendment to the claim) Claim 31 remains rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Claim 31 is directed to a conjugate comprising the peptide of claim 26, conjugated, linked or fused to a binding partner, in which the binding partner is selected from 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), a polyamino acids, a pharmacologically inactive proteins selected from albumin, gelatin, a fatty acid, polysaccharide, a lipid amino acid, dextran, a lipophilic group, or an antibody molecule; and a composition comprising such peptide.
As evidenced by the glutelin [Oryza sativa] document (1999, pages 1-2, from https://www.ncbi.nlm.nih.gov/protein/BAA36695.1?report=genbank&log$=protalign&blast_rank=1&RID=YB9NZT7S013, cited and enclosed in the previous office action), glutelin from Oryza sativa is a conjugate comprising the peptide of instant SEQ ID NO: 109 (amino acids 497-510 of glutelin) fused to a polyamino acids (amino acids 1-496 of glutelin), for example, the amino acid sequence on pages 1-2. And glutelin from Oryza sativa is a natural product.
The claim 31 does not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claimed conjugate in instant claim 31 does not recite features or steps demonstrating a marked difference from what exists in nature; and the claimed conjugate in claim 31 does not recite meaningful limitations that add something of significance to the judicial exception. Therefore, the claimed conjugate in instant claim 31 is not significantly different than a judicial exception (natural product).
Response to Applicant's Arguments
20. Applicant argues that “claim 31 is amended to remove the phrase "a molecular weight increasing compound" and to recite specific binding partners.”
21. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, as stated in Section 19 above, glutelin from Oryza sativa is a conjugate comprising the peptide of instant SEQ ID NO: 109 (amino acids 497-510 of glutelin) fused to a polyamino acids (amino acids 1-496 of glutelin), which is a conjugate recited in instant claim 31. And glutelin from Oryza sativa is a naturally occurring polypeptide. Therefore, the claimed conjugated recited in instant claim 31 is not significantly different than a judicial exception (natural product).
Thus, the rejection is deemed proper and is hereby maintained.
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
22. 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.
23. (Revised due to Applicant’s amendment to the claim) Claims 26 and 29-39 remain 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 and 29-39 recite an anti-inflammatory peptide comprising the amino acid sequence of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length; a conjugated comprising such peptide conjugated, linked or fused to a binding partner, in which the binding partner is selected from 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), a polyamino acids, a pharmacologically inactive proteins selected from 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 of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, 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.
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 examples of a peptide comprising the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length.
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 significant 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 of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, 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 examples of a peptide comprising the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alteration, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length.
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 significant 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 of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, 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 of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, 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
24. Applicant argues that “The working examples, as the Office Action acknowledges demonstrates both SEQ ID NOs: 109 and 320 reduce the secretion of TNFα. Comparison between two anti-inflammatory peptides is moot. Therefore, the instant specification provides adequate written description for the claimed genus..”
25. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, as stated in Section 23 above, first, the genus of instant claimed peptide is very broad, including any peptide comprising the amino acid sequence of SEQ ID NO: 109, or the amino acid sequence of SEQ ID NO: 109 having 1 to 3 amino acid alterations, wherein the amino acid alteration is independently selected from insertion, addition, deletion or substitution of an amino acid, and wherein the peptide is up to 50 amino acids in length. Second, with regards to the peptide of instant SEQ ID NO: 320 (a variant of the peptide of instant SEQ ID NO: 109 with K at position 14 deleted), the Examiner understands that the peptide of instant SEQ ID NO: 320 exhibits the activity of reducing the secretion of TNFα by 13%. However, such reduction is significant less than that of the peptide of instant SEQ ID NO: 109. Therefore, based on the limited examples presented in instant specification, 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. Furthermore, the data regarding the peptide of instant SEQ ID NO: 320 indicate that even a single amino acid change in the amino acid sequence of instant SEQ ID NO: 109 can have dramatic effects on the function of the peptide of instant SEQ ID NO: 109 being an anti-inflammatory peptide. Such data further confirm what is well known in the peptide/protein art, in 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 discussed in the cited Drumm et al and Yampolsky et al references.
Taken all these together, the rejection is deemed proper and is hereby maintained.
Claim Rejections - 35 U.S.C. § 102(a)(1)
26. 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.
27. (Revised due to Applicant’s amendment to the claim) Claim 31 remains rejected under 35 U.S.C. 102(a)(1) as being anticipated by the glutelin [Oryza sativa] document (pages 1-2, 1999, 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).
The instant claim 31 is drawn to a conjugate comprising the peptide of claim 26, conjugated, linked or fused to a binding partner, in which the binding partner is selected from 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), a polyamino acids, a pharmacologically inactive proteins selected from 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 glutelin [Oryza sativa] document teaches glutelin from Oryza sativa is a conjugate comprising the peptide of instant SEQ ID NO: 109 (amino acids 497-510 of glutelin) fused to a polyamino acids (amino acids 1-496 of glutelin), for example, the amino acid sequence on pages 1-2. It meets the limitation of instant claim 31.
Since the reference teaches all the limitations of instant claim 31; the reference anticipates instant claim 31.
Response to Applicant's Arguments
28. Applicant argues that “claim 31 is amended to remove the phrase "a molecular weight increasing compound" and to recite specific binding partners.”
29. Applicant's arguments have been fully considered but have not been found persuasive.
In response to Applicant's arguments about instant rejection, as stated in Section 27 above, glutelin from Oryza sativa is a conjugate comprising the peptide of instant SEQ ID NO: 109 (amino acids 497-510 of glutelin) fused to a polyamino acids (amino acids 1-496 of glutelin); and it meets all the limitations of the conjugate recited in instant claim 31.
Therefore, the rejection is deemed proper and is hereby maintained.
Examiner’s Notes
30. As stated in the previous office action, the peptide and the composition recited in instant claims 26, 28-30 and 32-39 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 action). 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 and the composition recited in instant claims 26, 28-30 and 32-39. Therefore, the peptide and the composition recited in instant claims 26, 28-30 and 32-39 are both novel and unobvious over the prior arts of record. And the claimed peptide and the composition are markedly different from what exist in nature.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
No claim is allowed.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658