Prosecution Insights
Last updated: September 17, 2026
Application No. 18/681,534

BIOMIMETIC PEPTIDES AND THEIR USE IN BONE REGENERATION

Non-Final OA §101§112
Filed
Feb 06, 2024
Priority
Aug 09, 2021 — IT 102021000021557 +1 more
Examiner
BORGEEST, CHRISTINA M
Art Unit
Tech Center
Assignee
Silk Biomaterials S R L
OA Round
1 (Non-Final)
56%
Grant Probability
Moderate
1-2
OA Rounds
6m
Est. Remaining
77%
With Interview

Examiner Intelligence

Grants 56% of resolved cases
56%
Career Allowance Rate
403 granted / 724 resolved
-4.3% vs TC avg
Strong +21% interview lift
Without
With
+21.3%
Interview Lift
resolved cases with interview
Typical timeline
3y 2m
Avg Prosecution
50 currently pending
Career history
766
Total Applications
across all art units

Statute-Specific Performance

§101
9.1%
-30.9% vs TC avg
§103
25.9%
-14.1% vs TC avg
§102
15.1%
-24.9% vs TC avg
§112
32.0%
-8.0% vs TC avg
Black line = Tech Center average estimate • Based on career data from 724 resolved cases

Office Action

§101 §112
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 . Status of the Claims The preliminary amendment filed 02/06/2024 is acknowledged. Claims 1, 3-6 and 10 are amended and claims 2, 9 and 11-13 are canceled. No restriction requirement is being imposed in this case. Claims 1, 3-8 and 10 are under examination. Priority Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Claim Interpretation The MPEP instructs that where a claim sets forth a plurality of elements, each element of the claim should be separated by a line indentation. In addition, there may be plural indentations to further segregate sub-combinations or related steps (see MPEP 608.01(m) and 37 CFR 1.75(i). Claim 1 recites peptides consisting of the general formula (1): Xaa1-Ser-Gly-Tyr-Glu-Tyr-Xaa2 (SEQ ID NO: 5), wherein: - when Xaa1 is Val-Asn-Gly-Gly-Tyr (SEQ ID NO:6), Xaa2 is Ala-Trp-Ser-Ser-Glu-Ser-Asp-Phe (SEQ ID NO:7) or Xaa2 is Ala-Trp; - when Xaa1 is absent, Xaa2 is Ala-Trp-Ser-Ser-Glu-Ser-Asp-Phe (SEQ ID NO:7); and - when Xaa1 is Gly-Pro-Tyr-Val-Ala-His-Gly-Gly-Tyr (SEQ ID NO:8), Xaa2 is absent. Each indentation of “-” followed by “when” is interpreted as a different element. The first element sets forth two possibilities: SEQ ID NO: 6 – SEQ ID NO: 5 – SEQ ID NO:7, which is equivalent to SEQ ID NO: 1; Or SEQ ID NO: 6 – SEQ ID NO: 5 – Ala-Trp, which is equivalent to SEQ ID NO: 4. The second element sets forth: SEQ ID NO: 5 (without Xaa1) – SEQ ID NO:7, which is equivalent to SEQ ID NO: 2. The third element sets forth: SEQ ID NO:8 – SEQ ID NO: 5 (without Xaa2), which is equivalent to SEQ ID NO: 3. Claim Objections Claims 1, 3 and 7 are objected to because of the following informalities. (i) Although claim 1 properly uses indentation to indicate different variants of the encompassed peptides, the indented dash is visually busy. The claim would benefit from numbering to indicate the different peptide variants. (ii) Claim 3 should recite “A [method of regenerating bone…”. (iii) There are unnecessary spaces in line 2 of claim 7 between “and” and “/” and “/” and “or”. Appropriate correction is required. Claim Rejections - 35 USC § 112(b) 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 applicant regards as his invention. Claims 3-5 and 10 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. Claim 3 recites a “[m]ethod of regenerating bone, dental and periodontal tissue in a subject in need thereof with the peptides according to claim 1” in the preamble followed by the step comprising: “forming hybrid composites with hydroxyapatite and said peptides”. The only required active step in this method of regenerating bone/dental/ periodontal tissue is forming hybrid composites with the peptides and hydroxyapatite, which describes a method of preparation, not treatment, as the preamble suggests. The clause “wherein said hybrid composites activate and accelerate nucleation and deposition of said hydroxyapatite in said bone, dental and periodontal tissue in said subject” does not clearly require any administering step and is interpreted as a description of an effect of the medicament. The claimed method is confusing because it does not clearly distinguish between a method of treatment and a method of preparing a medicament. Claims 4, 5 and 10 are hereby included in this rejection for depending upon an indefinite claim without resolving the indefiniteness. Claim Rejections - 35 USC § 101 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. Claims 1, 6, 7 and 8 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception without significantly more. The first step in considering patent eligibility is to establish the broadest reasonable interpretation of the claims as a whole and determine the statutory category of the claims (see Step 1 of the Revised Guidelines). The claims recite peptides and compositions comprising said peptides, thus are drawn to products. The first prong of the two-prong inquiry for determining whether a claim is patent eligible is to consider whether it is directed to a law of nature, a natural phenomenon (nature-based product) or an abstract idea. In evaluating whether the encompassed peptide/nucleotide is drawn to a nature-based product, the standard is whether or not the invention as claimed is markedly different from the closest corresponding product of nature, in this case full-length fibroin protein. See MPEP 2106(c)(II), which instructs how to conduct this analysis: The markedly different characteristics analysis compares the nature-based product limitation to its naturally occurring counterpart in its natural state. Markedly different characteristics can be expressed as the product’s structure, function, and/or other properties, and are evaluated based on what is recited in the claim on a case-by-case basis. If the analysis indicates that a nature-based product limitation does not exhibit markedly different characteristics, then that limitation is a product of nature exception. If the analysis indicates that a nature-based product limitation does have markedly different characteristics, then that limitation is not a product of nature exception. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the following reasons. The claims recite fragments of the full-length fibroin protein produced by the silkworm. See the amino acid sequence of the full-length protein with the recited peptide fragments either underlined or bolded: ID AAF76983; SV 1; linear; genomic DNA; STD; INV; 15792 BP. PA AF226688.1 DT 28-JUN-2000 (Rel. 64, Created) DT 28-JUN-2000 (Rel. 64, Last updated, Version 1) DE Bombyx mori (domestic silkworm) fibroin heavy chain Fib-H OS Bombyx mori (domestic silkworm) OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombycinae; Bombyx. FT source 1..15792 FT /organism="Bombyx mori" FT /strain="p50" FT /mol_type="genomic DNA" FT /db_xref="taxon:7091" FT CDS join(AF226688.1:62438..62479,AF226688.1:63451..79200) FT /codon_start=1 FT /gene="fib-H" FT /product="fibroin heavy chain Fib-H" FT /db_xref="PDB:3UA0" FT /db_xref="UniProtKB/Swiss-Prot:P05790" FT /protein_id="AAF76983.1" FT /translation="MRVKTFVILCCALQYVAYTNANINDFDEDYFGSDVTVQSSNTTDE FT IIRDASGAVIEEQITTKKMQRKNKNHGILGKNEKMIKTFVITTDSDGNESIVEEDVLMK FT TLSDGTVAQSYVAADAGAYSQSGPYVSNSGYSTHQGYTSDFSTSAAVGAGAGAGAAAGS FT GAGAGAGYGAASGAGAGAGAGAGAGYGTGAGAGAGAGYGAGAGAGAGAGYGAGAGAGAG FT AGYGAGAGAGAGAGYGAGAGAGAGAGYGAGAGAGAGAGYGAASGAGAGAGYGQGVGSGA FT ASGAGAGAGAGSAAGSGAGAGAGTGAGAGYGAGAGAGAGAGYGAASGTGAGYGAGAGAG FT YGGASGAGAGAGAGAGAGAGAGYGTGAGYGAGAGAGAGAGAGAGYGAGAGAGYGAGYGV FT GAGAGYGAGYGAGAGSGAASGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG FT SGAGAGSGAGAGSGTGAGSGAGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGA FT GSGAGAGSGAGAGSGAGAGYGAGAGAGYGAGAGAGYGAGAGVGYGAGAGSGAASGAGAG FT SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGVGYGAGV FT GAGYGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSRSDGYE FT YAWSSDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGVGYGAGY FT GAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG FT SGAGAGSGAGAGSGAGAGSGAGVGSGAGAGSGAGAGVGYGAGAGVGYGAGAGSGAASGA FT GAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGVGYG FT AGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGS FT GAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGAGYGAGYGAGAG FT AGYGAGAGSGAASGAGSGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGA FT GSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAG FT AGSGAGAGSGAGAGSGAGAGSGAGVGYGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGA FT GTGSSGFGPYVAHGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGA FT GYGAGVGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAG FT AGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGA FT GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYG FT AGAGSGAGSGAGAGSGAGAGSGAGAGSGAGVGSGAGAGSGAGAGSGAGAGSGAGAGYGA FT GYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAG FT AGSGAGVGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPY FT VANGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGA FT GAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSG FT AGSGSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAASGAGAGA FT GAGAGTGSSGFGPYVAHGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGSGAGA FT GSGAGAGSGAGAGSGAGAGYGAGVGAGYGAAYGAGAGAGYGAGAGSGAASGAGAGSGAG FT AGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGA FT GAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGSGAGAGSG FT AGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGYGAGAGA FT GYGAGYGAGAGAGYGAGAGTGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG FT SGAGSGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGAGYGAGYGAGA FT GAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGSGAASGAGAGAG FT AGAGTGSSGFGPYVAHGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGAGAGAGSGAGAG FT YGAGVGAGYGAGYGAGAGAGYGAGAGSGTGSGAGAGSGAGAGYGAGVGAGYGAGAGSGA FT AFGAGAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAG FT SGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGA FT GYGAGAGSGAASGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAG FT SGAGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSGYEYAWSSESDFGTG FT SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGA FT GSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGSGAASGAGAG FT SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGA FT GAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSG FT AGAGSGAGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSGAGA FT GSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAG FT AGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGA FT GSGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGVGAGYGAGAGSGAA FT SGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGV FT GAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGAGSGAGAGTGAGAGSGAGAGYGAG FT AGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSGYEYAWSSESDFGTGSGAGAGSGAG FT AGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGA FT GAGSGAGAGYGAGAGSGTGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGVG FT AGYGVGYGAGAGAGYGVGYGAGAGAGYGAGAGSGTGSGAGAGSGAGAGSGAGAGSGAGA FT GSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAG FT AGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGYGVGYGA FT GAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAG FT AGYGAGVGAGYGVGYGAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGA FT GAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGVGYGAG FT AGAGYGAGAGSGAASGAGAGAGAGAGTGSSGFGPYVANGGYSGYEYAWSSESDFGTGSG FT AGAGSGAGAGSGAGAGYGAGYGAGVGAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAGA FT GAGAGAGSGAGAGSGAGAGAGSGAGAGYGAGYGIGVGAGYGAGAGVGYGAGAGAGYGAG FT AGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGVGA FT GYGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGAGAGAGAGSGAGAGSGAGAGSGAGAG FT SGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGGAGAGYGAG FT AGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGSGAASGAGAGA FT GAGAGTGSSGFGPYVNGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGYGAGVG FT AGYGAGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGS FT GAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGYGAGAGAGYGAGAGSGAA FT SGAGAGSGAGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGA FT GYGAGYGAGVGAGYGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGSGSGAGSGAGAGSG FT AGAGSGAGAGAGSGAGAGSGAGAGSGAGAGYGAGYGAGAGSGAASGAGAGAGAGAGTGS FT SGFGPYVANGGYSGYEYAWSSESDFGTGSGAGAGSGAGAGSGAGAGYGAGVGAGYGAGY FT GAGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAG FT SGAGAGYGAGYGAGAGAGYGAGAGVGYGAGAGAGYGAGAGSGAGSGAGAGSGSGAGAGS FT GSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGYGIGVGAG FT YGAGAGVGYGAGAGAGYGAGAGSGAASGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGA FT GAGSGAGAGSGAGAGSGAGAGSGAGAGYGAGAGVGYGAGAGSGAASGAGAGSGAGAGSG FT AGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGSGAGAGSGAGAGYGAGYGAGVGAGYGA FT GAGYGAGYGVGAGAGYGAGAGSGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAGAGSGAG FT SGAGAGYGAGAGAGYGAGAGAGYGAGAGSGAASGAGAGAGAGSGAGAGSGAGAGSGAGS FT GAGAGSGAGAGYGAGAGSGAASGAGAGSGAGAGAGAGAGAGSGAGAGSGAGAGYGAGAG FT SGAASGAGAGAGAGTGSSGFGPYVANGGYSRREGYEYAWSSKSDFETGSGAASGAGAGA FT GSGAGAGSGAGAGSGAGAGSGAGAGGSVSYGAGRGYGQGAGSAASSVSSASSRSYDYSR FT RNVRKNCGIPRRQLVVKFRALPCVNC" The instant specification discloses that the peptides recited in claim 1 promote mineralization (see p. 11, lines 19-27). According to Kundu et al. (International Journal of Biological Macromolecules 153 (2020) 1328-1334), fibroin itself promotes mineralization. In addition, see Alessandrino (US20170312387), which describes preparing silk fibroin for use as an implantable medical device for use in regenerative medicine. In summary, the art provides evidence that the full-length protein has similar mineralization characteristics as the claimed peptide fragments. The courts have emphasized that to show a marked difference from a natural phenomenon, a characteristic in said phenomenon must be changed as compared to nature, and cannot be an inherent or innate characteristic of the naturally occurring counterpart or an incidental change in a characteristic of the naturally occurring counterpart. See Myriad, 569 U.S. at 580, 106 USPQ2d at 1974-75. Thus, in order to be markedly different, applicant must have caused the claimed product/ manufacture to possess at least one characteristic that is different from that of the naturally occurring counterpart. In the instant case, the isolation of fibroin peptide fragments (SEQ ID NOs: 1-4) from the full-length protein does not render the peptides markedly different from fibroin found in nature. In Myriad, the Supreme Court made clear that not all changes in characteristics will rise to the level of a marked difference, e.g., the incidental changes resulting from isolation of a gene sequence are not enough to make the isolated gene markedly different. In Myriad, 569 U.S. at 580, 106 USPQ2d at 1974-75, the patentee had discovered the location of the BRCA1 and BRCA2 genes in the human genome, and isolated them, i.e., separated those specific genes from the rest of the chromosome on which they exist in nature. As a result of their isolation, the isolated genes had a different structural characteristic than the natural genes, i.e., the natural genes had covalent bonds on their ends that connected them to the rest of the chromosome, but the isolated genes lacked these bonds. However, the claimed genes were otherwise structurally identical to the natural genes, e.g., they had the same genetic structure and nucleotide sequence as the BRCA genes in nature. Similar to Myriad, the isolation of peptides from the full-length fibroin that possess the same mineralization properties as the full-length protein does not render it markedly different from said natural products. The answer to Prong One of Step 2A is yes. The second step when determining patent eligibility is to consider whether the claims recite additional elements that integrate the natural phenomenon into a practical application (see MPEP 2106.04(d)(ll)). Claim 1 merely recites the peptide. Claim 6 recites “[a] composition comprising one or more peptides according to claim 1, their salts and excipients or additives acceptable in the biomedical, cosmetic or pharmaceutical field.” The instant specification does not define the excipients and additives, but one such common excipient is water, itself a natural product. Further, there is no evidence presented that the inclusion of the peptides in an excipient or its combination with an additive would change its properties. Claim 7 recites various further additives, but many of these, collagen, elastin, pectin sericin, cellulose, and fibrin, for example, are themselves naturally occurring products. Claim 7 even recites the inclusion of the full-length silk fibroin protein itself. There is no evidence in the specification or art that mixing the peptides with other agents integrates the natural phenomenon into a practical application. Likewise, the placement of the naturally occurring peptides in a gel, paste, powder or on a membrane, etc. as recited in claim 8 does not change the structure or function of the natural product. In summary, the inclusion excipients or placement in solution does not change the characteristics or function of the nature-based product and therefore does not integrate it into a practical application. The final step in the consideration of whether a claim is patent eligible is to consider whether there are additional elements in the claims sufficient to amount to significantly more than the judicial exception (see Step 2B of the Revised Guidelines). As noted above, claims 6, 7 and 8 do not recite any additional elements. Further, the inclusion of excipients such as in a pharmaceutical composition or formulation in a solution, is well-known, understood and routine in the pharmaceutical arts and does not add significantly more to the judicial exception. Thus claims 1, 6, 7 and 8 are not patent eligible. Note, however, that this issue could be addressed by amending the claims to recite that the peptides have been functionalized on fibroin foam (see p. 14, lines 10-20; p. 16, lines 7-14). Closest Prior Art Tsubouchi (7,193,038—on IDS filed 02/06/2024) disclose growth-promoting peptides derived from silk fibroin that encompass the recited sequences (see sequence listing). For example, the alignment between SEQ ID NO: 18 of Tsubouchi and instant SEQ ID NO: 1 is as follows: RESULT 1 US-10-789-494B-18 Sequence 18, US/10789494B Patent No. 7193038 GENERAL INFORMATION APPLICANT: TSUBOUCHI, Kozo APPLICANT: YAMADA, Hiromi TITLE OF INVENTION: EXTRACTION AND UTILIZATION OF CELL TITLE OF INVENTION: GROWTH-PROMOTING PEPTIDES FROM SILK PROTEIN FILE REFERENCE: OPS 635 CURRENT APPLICATION NUMBER: US/10/789,494B CURRENT FILING DATE: 2004-02-27 PRIOR APPLICATION NUMBER: JP 2003-55048 PRIOR FILING DATE: 2003-02-28 NUMBER OF SEQ ID NOS: 85 SEQ ID NO 18 LENGTH: 28 TYPE: PRT ORGANISM: Bombyx mori Query Match 100.0%; Score 102; Length 28; Best Local Similarity 100.0%; Matches 18; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 VNGGYSGYEYAWSSESDF 18 |||||||||||||||||| Db 9 VNGGYSGYEYAWSSESDF 26 Nevertheless, the prior art does not teach or suggest the peptides consisting of the general formula recited in claim 1. Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA M BORGEEST whose telephone number is (571)272-4482. The examiner can normally be reached M-F 9-5:30 EDT. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at 5712720911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. 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. /CHRISTINA M BORGEEST/Primary Examiner, Art Unit 1675
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Prosecution Timeline

Feb 06, 2024
Application Filed
Aug 25, 2026
Non-Final Rejection mailed — §101, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
56%
Grant Probability
77%
With Interview (+21.3%)
3y 2m (~6m remaining)
Median Time to Grant
Low
PTA Risk
Based on 724 resolved cases by this examiner. Grant probability derived from career allowance rate.

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