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 .
Withdrawal of Rejections
The response and amendments filed on 06/09/2026 are acknowledged. Any previously applied minor objections and/or minor rejections (i.e., formal matters), not explicitly restated here for brevity, have been withdrawn necessitated by Applicant’s formality correction and/or amendments. For the purposes of clarity of the record, the reasons for the Examiner’s withdrawal, and/or maintaining, if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner’s Response to Arguments section.
Briefly, the previous claim rejections under 35 U.S.C 112(b) for claim 1 has been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection are set forth below. The previous claim rejections under 35 U.S.C. 112(a) for written description have been withdrawn necessitated by Applicant’s amendments. The previous claim rejections under 35 U.S.C. 102 for anticipation have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection are set forth below.
The following rejections and/or objections are either reiterated or newly applied. They constitute the complete set presently being applied to the instant application.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 06/09/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Objections
Claim 1 is objected to because of the following informalities: “35 kD” should be “35 kDa”. Appropriate correction is required.
New Grounds of Rejection Necessitated by Amendments and/or Maintained Rejections
Claim Rejections - 35 USC § 112(b), Indefiniteness
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 3 and 7 are rejected under 35 U.S.C. 112(b) 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 the limitation "the procuring step". There is insufficient antecedent basis for this limitation in the claim. No procuring step was previously recited.
Claim 7 recites “the release profile”. There is insufficient antecedent basis for this
limitation in the claim. No release profile was previously recited. Moreover, it is unclear what a
“release profile” means, as there is no definition in the instant specification for this term. It is
unclear if the release profile simply refers to the peptide’s release from the collagen, or if the release profile refers to how much peptide is released from the collagen and interacts with a cell
of interest over time, or if the release profile refers to how much peptide is released from the
collagen and exhibits a desired effect. Therefore, this is indefinite because it is unclear what a
release profile is in terms of the peptide and the metes and bounds of the claimed invention
cannot be readily ascertained since this is not defined in the instant specification (see, e.g.,
MPEP 2173.02). For the purposes of applying prior art, the Examiner has interpreted “release
profile” to be the concentration of peptides needed to exhibit a desired effect.
Claims 2, 4-6, and 8-9 are included in this rejection for depending on rejected independent claim 1 and failing to rectify the noted deficiency.
Examiner’s Response to Arguments
Regarding Applicant’s arguments pertaining to the previous 35 U.S.C 112(b) rejections for claim 1 (remarks, page 7), as stated above, all previous 35 U.S.C. 112(b) rejections for claim 1 have been withdrawn necessitated by Applicant’s amendments; however, new grounds of rejection are set forth above. Additionally, the 35 U.S.C. 112(b) rejection for claim 7 has been maintained because there is insufficient antecedent basis for “the release profile” and it is unclear what “release profile” means, as there is no definition in the specification.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 112(a), New Matter
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-9 are rejected under 35 U.S.C. 112(a) 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 molecular weight of about 20 kDa and 35 kDa”; however, there is no support in the instant specification for molecular weight of the peptides that are about 20 kDa and 35 kDa because this would encompass molecular weights above and below 20 kDa and 35 kDa and the instant specification does not provide support for molecular weights above and below 20 kDa and 35 kDa.
Claims 2-9 are included in this rejection for depending on rejected independent claim 1 and failing to rectify the noted deficiency.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 102, Anticipation
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-6 and 9 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Felician (The wound healing potential of collagen peptides derived from the jellyfish Rhopilema esculentum; 2019 – newly cited).
Felician’s general disclosure relates to investigating “the wound healing activity of collagen peptides derived from jellyfish following oral administration” (see, e.g., Felician, Abstract). Moreover, Felician discloses “collagen was extracted from the jellyfish–Rhopilema esculentum using 1% pepsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fourier transform infrared (FTIR) were used to identify and determine the molecular weight of the jellyfish collagen. Collagenase II, papain and alkaline proteinase were used to breakdown jellyfish collagen into collagen peptides. Wound scratch assay (in vitro) was done to determine migration potential of human umbilical vein endothelial cells (HUVEC) covering the artificial wound created on the cell monolayer following treatment with collagen peptides. In vivo studies were conducted to determine the effects of collagen peptides on wound healing by examining wound contraction, re-epithelialization, tissue regeneration and collagen deposition on the wounded skin of mice” (see, e.g., Felician, Abstract).
Regarding claim 1 pertaining to forming a targeted collagen product, Felician teaches that collagen was extracted from the jellyfish–Rhopilema esculentum using 1% pepsin and that collagenase II, papain, and alkaline proteases were used to digest the jellyfish collagen into collagen peptides (see, e.g., Felician, Methods, pgs. 13-14). Furthermore, Felician teaches production of collagen peptides between 10 kDa and ~40kDa, including peptides at molecular weights of 20 kDa and 35 kDa (see, e.g., Felician, Figure 3). Moreover, Felician teaches that the peptides exhibit wound healing capabilities, wherein the peptides were added to wounded mice, which inherently have collagen, and the peptides decreased wound area on the mice signifying wound healing capabilities (see, e.g., Felician, “In vivo wound healing activity”, pg. 17). Therefore, addition of the peptides to the mice, which inherently have collagen, would inherently lead to formation of the targeted collagen product.
Regarding claim 2 pertaining to digesting the source collagen to obtain peptides, Felician teaches collagen was extracted from the jellyfish–Rhopilema esculentum using 1% pepsin and that collagenase II, papain, and alkaline proteases were used to digest the jellyfish collagen into collagen peptides (see, e.g., Felician, Methods, pgs. 13-14).
Regarding claim 3 pertaining to the source collagen, Felician teaches that the source collagen is collagen extracted from the jellyfish–Rhopilema esculentum (see, e.g., Felician, Methods, pgs. 13-14), which is a eukaryote.
Regarding claim 4 pertaining to testing the peptides, Felician teaches testing the peptides for in vitro and in vivo wound healing, wherein the peptides derived from the jellyfish collagen exhibited wound healing capabilities (see, e.g., Felician, “In vitro wound healing activity”, pgs. 16-17 & “In vivo wound healing activity”, pgs. 17-18).
Regarding claim 5 pertaining to isolating the peptides exhibiting the desired characteristics, Felician teaches that the collagen peptides derived from jellyfish exhibit wound healing capabilities (see, e.g., Felician, “In vitro wound healing activity”, pgs. 16-17 & “In vivo wound healing activity”, pgs. 17-18). These peptides were isolated from jellyfish collagen, wherein “The extracted collagen (1 g) was suspended in 200 mL of ultra purified water and put in a water bath at 37C. Collagenase II enzyme (5% w/w) was then added and the mixture was stirred for 5h. The enzymatic reaction was terminated by heating the mixture at 95C for 10 min. The mixture was then cooled at room temperature and centrifuged at 3000 rpm for 30 min. The resulting supernatant was freeze-dried as collagen peptides CP1 and stored at 4C for further experimental use” (see, e.g., Felician, “Preparation of collagen peptides (CP1)”, pgs. 13-14).
Regarding claim 6 pertaining to adding the peptides to a precursor collagen to form the targeted collagen product, Felician teaches that the peptides exhibit wound healing capabilities, wherein the peptides were added to wounded mice, which inherently have collagen, and the peptides decreased wound area on the mice (see, e.g., Felician, “In vivo wound healing activity”, pg. 17). Addition of the peptides to the mice, which inherently have collagen, would inherently lead to formation of the targeted collagen product.
Regarding claim 9 pertaining to the precursor collagen, Felician teaches that the precursor collagen is from filaments of jellyfish (see, e.g., Felician, “Extraction of collagen (jellyfish collagen)”, pg. 13).
Examiner’s Response to Arguments
Regarding Applicant’s argument that Harrell, Lee I, and Lee II do not teach the amended claims (remarks, pages 7-8), as discussed above, all previous 35 U.S.C. 102 rejections have been withdrawn; however, new grounds of rejection are set forth above. Harrell, Lee I, and Lee II were not relied upon in the above presented rejection; therefore, Applicant’s arguments are moot.
New Grounds of Rejection Necessitated by Amendments
Claim Rejections - 35 USC § 103, Obviousness
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 7-8 are rejected under 35 U.S.C. 103 as being unpatentable over Felician as applied to claims 1-6 and 9 above, and further in view of Lee (Prolonged survival of transplanted stem cells after ischaemic injury via the slow release of pro-survival peptides from a collagen matrix; 2018 – previously cited).
The previous teachings of Felician are discussed above.
However, Felician does not teach: wherein the adding step is performed so that the reconstituted precursor collagen can control the release profile of the peptides exhibiting the desired characteristic (claim 7); or wherein the adding step is performed so that the reconstituted precursor collagen is crosslinked to the peptides exhibiting the desired characteristic (claim 8).
Lee’s general disclosure relates to covalently crosslinking peptide analogues to
collagen matrix scaffolds via dendrimers in order to improve the half-life of peptide analogues
(see, e.g., Lee, Introduction, pg. 104). Furthermore, Lee discloses the peptide analogues are
BMP2, EPO, and FGF2; therefore the “col×D×pep cocktail contained a combination of BMP2,
EPO and FGF2 individually crosslinked to dendrimized collagen (for example, col×D×BMP2,
col×D× EPO and col×D× FGF2)” (see, e.g., Lee, Introduction, pg. 104), wherein D
represents dendrimer.
Regarding claim 7 pertaining to the release profile of the peptides, Lee teaches
crosslinking collagen and peptides via dendrimers (see, e.g., Lee, Introduction, pg. 104),
wherein the crosslinked peptides demonstrated prolonged release that lasts for “periods longer
than 15 day” (see, e.g., Lee, “Gradual release of peptide factors from the colxDxpep
delivery system”, pg. 105). Moreover, Lee teaches “Interestingly, dendrimer crosslinking
resulted in different release profiles for different peptides, possibly due to the differential
alterations in collagen structure and charges (Fig. 2a–c). The slowest release profile, however,
was observed only when peptides were covalently crosslinked (Fig. 2d)” (see, e.g., Lee,
“Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105). Additionally,
Lee teaches “Peptides covalently crosslinked are released gradually as collagen degrades
and autolysis occurs. The presence of the dendrimer moieties promotes hydrolysis of the amide bonds24,25, fostering peptide release (Supplementary Fig. 9). Of the two cleavable sites
(dendrimer–peptide and dendrimer–collagen), the dendrimer–peptide link has greater exposure to
solvent, is more accessible for chemical transformations and is thus more prone to autolysis.
After autolytic cleavage, the release kinetics depends on the binding affinity of the peptide to
dendrimers in col× D, which varies according to the number of hydrogen donor groups in each
peptide. The quicker release of peptides from col× D + peptide compared to col + peptide is
probably due to the low binding affinity of peptides to the highly positively charged dendrimers
present in col× D (Fig. 2a–c)” (see, e.g., Lee, “Gradual release of peptide factors from the
colxDxpep delivery system”, pg. 105).
Regarding claim 8 pertaining to crosslinking the peptides to the precursor collagen, Lee teaches crosslinking collagen and peptides via dendrimers (see, e.g., Lee, Introduction, pg. 104), wherein the crosslinked peptides demonstrated prolonged release that lasts for “periods longer than 15 day” (see, e.g., Lee, “Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add the jellyfish collagen-derived peptides to the precursor collagen, as taught by Felician, wherein the adding step controls the release profile of the peptide(s), as taught by Lee. One would have been motivated to do so because Lee teaches crosslinked peptides demonstrated prolonged release that lasts for “periods longer
than 15 day” (see, e.g., Lee, “Gradual release of peptide factors from the colxDxpep
delivery system”, pg. 105). Moreover, Lee teaches “Interestingly, dendrimer crosslinking
resulted in different release profiles for different peptides, possibly due to the differential
alterations in collagen structure and charges (Fig. 2a–c). The slowest release profile, however,
was observed only when peptides were covalently crosslinked (Fig. 2d)” (see, e.g., Lee,
“Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105). Furthermore, Lee teaches “The quicker release of peptides from col× D + peptide compared to col + peptide is
probably due to the low binding affinity of peptides to the highly positively charged dendrimers
present in col× D (Fig. 2a–c)” (see, e.g., Lee, “Gradual release of peptide factors from the
colxDxpep delivery system”, pg. 105). Additionally, Lee teaches that peptides crosslinked to collagen via dendrimers would result in a controlled delivery system due to the release profile of the peptides from the collagen (see, e.g., Lee, Introduction, pg. 104). Therefore, Lee teaches that adding the peptides to the collagen, wherein the peptides are crosslinked to the collagen, controls the release profile of the peptides from the collagen. Moreover, Felician teaches that the peptides exhibit wound healing capabilities were added to wounded mice, which inherently have collagen, and the peptides decreased wound area on the mice (see, e.g., Felician, “In vivo wound healing activity”, pg. 17). Therefore, based on the teachings of Felician and Lee, it would have been obvious to crosslink the peptides to collagen via dendrimers in order to control the release profile of the peptides for production of a controlled delivery system for wound healing. One would have expected success because Felician and Lee both teach peptides that bind to collagen.
New Grounds of Rejection Necessitated by Amendments
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.
Claims 1 and 8 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/091,782 (reference application; herein referred to as “App’782”) in view of Felician (The wound healing potential of collagen peptides derived from the jellyfish Rhopilema esculentum; 2019 – newly cited).
Although the claims at issue are not identical, they are not patentably distinct from each other because App’782 claims: A method for forming a targeted collagen product having an amplified desired characteristic, comprising: adding peptides exhibiting a desired characteristic to collagen to form the targeted collagen product; wherein the adding step includes adding the peptides exhibiting the desired characteristic to a mixture to modify collagen into the targeted collagen product; wherein the adding step is performed so that the modified collagen is crosslinked to the peptide exhibiting the desired characteristic and wherein the crosslinking of the collagen to the peptide exhibiting the desired characteristic occurs by modification of the peptide to facilitate binding to the collagen (see, e.g., App’782, claim 1).
However, App’782 does not claim: wherein the peptides are P20 or P35 peptides having a molecular weight of 20 kDa and 35 kDa, respectively, and wherein the peptides exhibit a desired characteristic selected from the group consisting of wound healing, osteogenesis, blood clotting, organ scaffolds, dura repair, nerve repair, ocular repair, epithelial repair, cardio-vascular repair, breast repair, and endothelial repair.
Felician teaches a peptides isolated from jellyfish collagen, wherein these peptides have molecular weights between ~10kDa and ~40 kDa (see, e.g., Felician, Figure 3) and wherein these peptides exhibit wound healing capabilities (see, e.g., Felician, “In vitro wound healing activity”, pgs. 16-17 & “In vivo wound healing activity”, pgs. 17-18). Moreover, Felician teaches that “Different enzyme treatment on collagen can result into different products exhibiting similar or different bioactivities” (see, e.g., Felician, pg. 16)
Therefore, based on the teachings of Felician, it would have been obvious to claim a 20 kDa or 35 kDa peptide derived from a source collagen because these peptides, depending on the enzyme treatment, can exhibit different or similar biological properties, such as the wound healing properties exhibited by the jellyfish collagen-derived peptides taught by Felician.
This is a provisional nonstatutory double patenting rejection.
Conclusion
Claims 1-9 are rejected.
No claims are allowed.
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.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
