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 .
Claims Status
Claims 1-13 are pending.
Claims 1-11 are amended.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 04/22/2024 and 03/18/2024 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered.
Claim Objections
Claim 9 objected to because of the following informalities:
Claim 9 is dependent on a rejected claim. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 7 is 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.
With regards to claim 7, the claim recites “the reaction takes place in aqueous…”. There is lack of antecedent basis for “the reaction” which renders the claim indefinite.
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 4 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 4 is directed to all possible hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9. There is no disclosure of any particular structure to function/activity relationship in the disclosed species.
Collagen plays a central role in tissue architecture, extracellular matrix organization, and signal transduction. A structural feature that is common to all collagen is the unique triple helical structure composed of three left-handed polyproline-II-like chains that are supercoiled into a right handed helix. The close packing of the polypeptide helices near the central axis is made possible by having repeated glycine residues as every third residue, leading to a characteristic, repeating pattern (Gly-Xaa-Yaa). While the structure and biophysical properties of metazoan collagen were explored extensively in the scientific literature, discoveries in bacterial collagen are a burgeoning field for intensive research. (see pg. 3778, Qiu et al., ACS Biomaterials Science and Engineering, Vol. 9, pg. 3778-3795; published April 19, 2021; PMID: 33871954). Proteins containing large regions of Gly-Xaa-Yaa (GXY) repeats were uncovered in numerous bacterial genome databases, however, only a small fraction of the predicted bacterial collagen-like proteins was investigated so far. Additionally, distinct amino acid compositions for bacterial collagen-like proteins confer different mechanisms for imparting stability to collagenous triple-helical structures as bacteria lack the prolyl-4-hydroxylase and hydroxyproline responsible for the stability of triple helices. New production techniques are needed to overcome difficulties in aggregating bacterial collagens (see pg. 3789, Qiu et al., ACS Biomaterials Science and Engineering, Vol. 9, pg. 3778-3795; Epub April 19, 2021; PMID: 33871954).
Regarding the level of skill and knowledge in the art of amino acid mutation, the reference of Singh et al., (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached PTO0-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see pg. 7, column 1, top). Also, the unpredictability associated with amino acid mutations is exemplified by the reference of Zhang et al. (Structure 26: 1474-1485, 2018, cited on the attached Form PTO-82) which discloses that even a mutation of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
Given this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Claim 4 rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
Claim 4 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like protein is a polypeptide with the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9, does not reasonably provide enablement for all possible hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required, are summarized in In re Wands (858 F.2d 731, 8 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claim(s).
Claim 4 is so broad as to encompass all possible hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9.
The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the required variant polypeptides encompassed by the claims. Since the amino acid sequence of a protein determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. However, in this case the disclosure is limited to:
(claim 4) hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like protein is a polypeptide with the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9, does not reasonably provide enablement for all possible hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like polypeptide is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9.
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass any possible:
(claim 4) hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9.
because the specification does not establish: (A) regions of the polypeptide which may be modified affecting the polypeptide of claim 1; (B) the general tolerance of enzymes of the polypeptide of claim 1 to modification and extent of such tolerance; (C) a rational and predictable scheme for modifying any amino acid residue of a protein of the polypeptide of claim1 protein group with an expectation of obtaining the desired biological function; and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. Because of this lack of guidance, the extended experimentation that would be required to determine which substitutions would be acceptable to retain the required functions of the polypeptide of claim 1 and the fact that the relationship between the sequence of a peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (e.g., see Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495; Franceus et al., J. Ind. Microbiol. Biotechnol. Vol 44, pp 687-695, 2017), it would require undue experimentation for one skilled in the art to arrive at the majority of polypeptides having the function of the polypeptide of claim 4 of the claimed genus.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including any:
(claim 4) hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9.
The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of:
(claim 4) all possible hydrogels obtained by reacting at least one collagen-like protein and at least one cross-linker comprising at least two groups each comprising a polyalkylene glycol moiety and a succinimidyl group, wherein the bacterial collagen-like protein is a polypeptide that is at least ≥ 60% identical to the amino acid sequence of SEQ ID NO:1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, or SEQ ID NO: 9, is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-5, 7, and 10-13 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Ramshaw et al. (US Patent No: US 10,155,793 B2; published December 18, 2018), hereinafter referred to as Ramshaw.
With regards to claim 1, Ramshaw discloses a collagen-like protein can be produced in any form ranging from highly soluble forms to highly cross-linked forms such as hydrogels (see Collagen-like Protein of the Disclosure, Column 16, lines 55-58). Ramshaw discloses a collagen-like protein that is chemically reacted with an agent to provide a modified collagen-like protein wherein the chemical reaction induces cross-linking of reactive amino acid residues (see claims 1,7, and 8, Columns 61 and 62). ). Ramshaw discloses that the collagen-like protein is reacted with bis-maleimidyl (PEG)2 (comprises a polyalkylene glycol moiety and succinimidyl group) (see Example 13, pg. Column 27, lines 47-65). Ramshaw discloses that by increasing the extent of cross-linking, it is possible to generate hydrogels (a hydrogel obtained) which have various medical and non-medical applications (see column 6, lines 50-53).
With regards to claim 2, in addition to the teachings of Ramshaw as applied to claim 1 above, Ramshaw discloses a collagen-like protein comprising one or more bacterial triple-helical domains (see claim 1, column 61, lines 1-3) and that the disclosure provides modified bacterial collagen-like proteins that can be readily produced by recombinant means (see Summary of the Disclosure, column 3, lines 14-17).
With regards to claim 3, in addition to the teachings of Ramshaw as applied to claim 2 above, Ramshaw discloses a purified, modified, bacterial (S. pyogenes) collagen domain protein after cross-linking with bis-maleimidyl-PEG2 (see Figure 5, and Description of the figures, Column 12, lines 35-45). Ramshaw discloses that organisms which the bacterial collagen-like sequence can be derived include S. pyogenes (see Column 10, lines 11-17).
With regards to claim 4, in addition to the teachings of Ramshaw as applied to claim 1 above, Ramshaw discloses the sequence of a modified bacterial collagen-like protein (SEQ ID NO: 7) which shares 99.3% sequence identity with SEQ ID NO. 1 of the current instant application (see alignment below).
RESULT 3
US-15-024-290C-7
Sequence 7, US/15024290C
Patent No. 10155793
GENERAL INFORMATION
APPLICANT: Commonwealth Scientific and Industrial Research
TITLE OF INVENTION: Modified bacterial collagen-like proteins
FILE REFERENCE: 520336
CURRENT APPLICATION NUMBER: US/15/024,290C
CURRENT FILING DATE: 2016-03-24
PRIOR APPLICATION NUMBER: 2013903444
PRIOR FILING DATE: 2013-09-09
NUMBER OF SEQ ID NOS: 26
SEQ ID NO 7
LENGTH: 331
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: chemically synthesized bacterial collagen sequence
Query Match 99.3%; Score 1811; Length 331;
Best Local Similarity 100.0%;
Matches 328; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 NHKVHMHHHHHHADEQEEKAKVRTELIQELAQGLGGIEKKNFPTLGDEDLDHTYMTKLLT 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 NHKVHMHHHHHHADEQEEKAKVRTELIQELAQGLGGIEKKNFPTLGDEDLDHTYMTKLLT 61
Qy 61 YLQEREQAENSWRKRLLKGIQDHALDLVPRGSPGLPGPRGEQGPTGPTGPAGPRGLQGLQ 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 YLQEREQAENSWRKRLLKGIQDHALDLVPRGSPGLPGPRGEQGPTGPTGPAGPRGLQGLQ 121
Qy 121 GLQGERGEQGPTGPAGPRGLQGERGEQGPTGLAGKAGEAGAKGETGPAGPQGPRGEQGPQ 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 122 GLQGERGEQGPTGPAGPRGLQGERGEQGPTGLAGKAGEAGAKGETGPAGPQGPRGEQGPQ 181
Qy 181 GLPGKDGEAGAQGPAGPMGPAGERGEKGEPGTQGAKGDRGETGPVGPRGERGEAGPAGKD 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 182 GLPGKDGEAGAQGPAGPMGPAGERGEKGEPGTQGAKGDRGETGPVGPRGERGEAGPAGKD 241
Qy 241 GERGPVGPAGKDGQNGQDGLPGKDGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQD 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 242 GERGPVGPAGKDGQNGQDGLPGKDGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQD 301
Qy 301 GKDGLPGKDGKDGLPGKDGKDGQPGKPG 328
||||||||||||||||||||||||||||
Db 302 GKDGLPGKDGKDGLPGKDGKDGQPGKPG 329
With regards to claim 5, in addition to the teachings of Ramshaw as applied to claim 2 above, Ramshaw discloses that a nucleic acid sequence encoding the collagen-like proteins can be produced in a non-animal host cell, including bacterial or yeast cells (see Summary of the disclosure, Column 3, lines 24-27) and that post-expression cultured cells can be harvested (see Column 19, lines 10-12).
With regards to claim 7, in addition to the teachings of Ramshaw as applied to claim 1 above, Ramshaw discloses that a solution (aqueous) of the purified protein was adjusted to pH 6.8 (see Example 13, Column 27, lines 55-58).
With regards to claims 10-11, in addition to the teachings of Ramshaw as applied to claim 1 above, Ramshaw discloses that the collagen-like proteins can be stabilized by chemical fixation and reconstituted in various products (article) such as gel-like materials (hydrogel) and may be utilized in various applications such as membrane-like materials for use in anti-adhesion membranes, drug carriers, implant coatings, gel-like materials, wound treatment and management, wound dressings, adhesion barriers, and sponge-like materials (see Column 22,lines 45-66 and Column 23, lines 1-30).
With regards to claim 12, in addition to the teachings of Ramshaw as applied to claim 1 above, Ramshaw discloses that the sequences which are suitable for use in the generation of collagen-like proteins may be recombinantly derived from native triple-helical proteins found in bacterial organisms such as a bacterial collagen-like protein from Streptococcus pyogenes Sc12 (see Collagen-Like protein of the disclosure, Column 17, lines 8-14).
With regards to claim 13, in addition to the teachings of Ramshaw as applied to claim 5 above, Ramshaw discloses that bacterial host cell may be selected from E. coli and the yeast host cell may be selected from Pichia pastoris (see Column 9, lines 52-65 and Column 10, lines 3-7).
Therefore, claims 1-5, 7, and 10-13 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Ramshaw et al. (US Patent No: US 10,155,793 B2; published December 18, 2018).
Claims 1, 6-8, and 11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Fibrogen, Inc. (US Patent Application No: US 2006/0258560 A1; published November 16, 2006), hereinafter referred to as Fibrogen.
With regards to claim 1, Fibrogen discloses a tissue sealant composition which includes a crosslinking agent and further includes a combination of a synthetic collagen (collagen-like protein) and synthetic gelatin (hydrogel) whereas upon contact with an environment comprising a physiological pH, the crosslinking agent reacts with the synthetic collagen or synthetic gelatin (hydrogel obtained) to form a tissue sealant composition (see Paragraph 008) . Fibrogen discloses a sealant comprising a synthetic gelatin (hydrogel) comprising a synthetic collagen (see Production of Recombinant Collagen, Paragraph 0119, pg. 15) (collagen-like protein sequence shown below).
>US-10-529-708-3 DRY TISSUE SEALANT COMPOSITIONS
QYDSYDVKAGVAVGGLAGYPGPAGPPGPPGPPGAAGHPGSPGSPGYQGPPGEPGQAGPSG
PPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNG
EKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPG
PPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPG
GKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAG
IPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPG
PAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRG
QPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGEAGPQGPPGPAGPGGDKGDTG
PPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPG
LRGGAGPPGPEGGKGAAGPPGPPGAAGAPGLQGMPGERGGLGAPGPKGDKGEPGGPGADG
VPGKDGPRGPAGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGEAGPPGPAGFPG
APGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAG
FPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNAGAPGAPGVSGPKGDAGQPGEKG
SPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERG
PPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPG
PVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPG
NPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERG
SEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIA GIGGEKAGGFAPYYGDEPMDFKINTDE
IMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVF
CNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVQ
LAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVL
EDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL
Fibrogen discloses that the crosslinking agent and the synthetic collagen or synthetic gelatin comprise a mixture and the crosslinker is a PEG-succinimidyl ester that is PEG-succinimidyl propionate (comprises polyalkylene glycol moiety and succinimidyl group) or PEG-succinimidyl glutarate (see claims 9-12, pg. 28-29).
With regards to claims 6-8, in addition to the teachings of Fibrogen as applied to claim 1 above, Fibrogen discloses that the effect of the ratio of human recombinant gelatin and crosslinking agent on gelation time was analyzed. 100 mg/mL of recombinant human collagen type III was dissolved in phosphate buffer, pH 8.0 and mixed with various amounts of 8-arm PEG- succinimidyl propionate (has formulae (I) of claim 6 of the current instant application (see Example 4, Paragraphs 0108-0109, pg. 13-14).
With regards to claim 11, in addition to the teachings of Fibrogen as applied to claim 1, Fibrogen discloses a tissue sealant (article) comprising a sealant mixture comprising a synthetic gelatin or synthetic collagen, and crosslinking agent and at least one agent suitable to provide a therapeutic benefit in sealing the wound (see Paragraph 0077, pg. 9).
Therefore, claims 1, 6-8, and 11 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Fibrogen, Inc. (US Patent Application No: US 2006/0258560 A1; published November 16, 2006).
The prior art made of record and not relied upon is considered pertinent to the applicant’s disclosure.
Qiu et al. “Current Insights on the Diverse Structures and Functions in Bacterial Collagen-like Proteins”, ACS Biomater Sci Eng, Vol. 9, pg. 3778-3795; Epub April 19, 2021; PMID: 33871954.
provides a review of the latest insight into the functional and structural diversity from multiple perspectives of biology, computational simulations, and materials engineering of bacterial collagen-like proteins.
Merrett et al. “Enhanced Collagen-like Protein for Facile Biomaterial Fabrication”, ACS Biomater Sci Eng., Vol. 7, pg. 1414-1427; Epub March 18, 2021; PMID: 33733733
teaches a collagen-mimetic protein of bacterial origin based upon a modified subdomain of the collagen-like Sc12 protein from Streptococcus pyogenes.
Cosgriff-Hernandex et al. “Bioactive hydrogels based on designer collagens”. Acta Biomater., Vol. 6, pg. 3969-3977; published October 2010, PMID: 20466083
teaches bioactive hydrogels that were fabricated by combining functionalized Sc12 proteins with poly(ethylene glycol) diacrylate and photocrosslinking.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to GEORGE T LOUNTOS whose telephone number is (571)272-0502. The examiner can normally be reached Monday-Friday 8:00 am - 5:00 pm.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
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