DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-3 are pending and are being examined on the merits.
Priority
This application is filed under 35 U.S.C. 121 as a divisional application of U.S. non-provisional application no. 16/942,552, filed July 29, 2020, which is filed under 35 U.S.C. 120 as a continuation of international application PCT/JP2019/002869, filed January 29, 2019, which claims foreign priority under 35 U.S.C. 119(a)-(d) to Japanese application no. 2018-013283, filed January 30, 2018. A certified copy of the foreign priority document has been filed in this application on August 23, 2024.
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d), a certified English translation of the foreign priority application must be submitted. Failure to provide a certified translation may result in no benefit being accorded for the non-English application.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on August 9, 2024 and October 11, 2024 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDSs have been considered by the examiner.
Claim Objections
Claim 1 is objected to because of the following informalities:
Claim 1 is objected to for reciting “subjecting the mixture of the blocks and blood to centrifugation; wherein, an anticoagulant is not present in the fibrin composition” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite (with markings to show changes) “subjecting the mixture of the blocks and blood to centrifugation to thereby manufacture a fibrin composition comprising blocks, fibrin and platelets; wherein, an anticoagulant is not present in the fibrin composition.”
Claim 1 is also objected to for reciting “wherein the protein is any of a peptide” and in the interest of improving claim form and consistency, it is suggested that the term “peptide” in claim 1 be replaced with “protein.”
Claim 1 is also objected to for reciting “sequence described in SEQ ID NO: 1” and in the interest of improving claim form and consistency, it is suggested that the noted phrase be amended to recite (with markings to show changes) “sequence of
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.
Claims 1-3 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 regards as the invention.
Claim 1 (claims 2-3 dependent therefrom) is indefinite in the recitation of “a peptide…having biocompatibility” because it is unclear as to what the recited “peptide” has biocompatibility. It is suggested that applicant clarify the meaning of the phrase “having biocompatibility.”
Claim 3 is indefinite in the recitation of “wherein in the blocks” because it is unclear as to the “blocks” in claim 1 (i.e., the frozen blocks, the blocks following freeze-drying pulverizing of the frozen blocks, and/or the sieved blocks) that is/are referenced by the noted phrase. It is suggested that applicant clarify the meaning of claim 3 by identifying the “blocks” in claim 1 that is/are referenced by the noted phrase.
Claim Rejections - 35 USC § 112(a)
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.
Claims 1-3 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 at the time the application was filed, had possession of the claimed invention.
MPEP 2163.II.A.2.(a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the 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”.
For claims drawn to a genus, MPEP § 2163 states the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
MPEP § 2163 further states that “[s]atisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’ Such correlations may be established ‘by the inventor as described in the specification,’ or they may be ‘known in the art at the time of the filing date.’"
The factors considered in the Written Description requirement are (1) level of skill and knowledge in the art, (2) partial structure, (3) physical and/or chemical properties, (4) functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the (5) 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.
The claims recite a genus of peptides consisting of an amino acid sequence described in SEQ ID NO: 1, a genus of peptides having an amino acid sequence, which is obtained by the deletion, substitution, or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility, and a genus of peptides having an amino acid sequence, which shares sequence identity equal to or higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility.
Regarding the recited genus of peptides consisting of an amino acid sequence described in SEQ ID NO: 1, the recitation of “an amino acid sequence” in the phrase “an amino acid sequence described in SEQ ID NO: 1” is interpreted as any two or more contiguous amino acids of SEQ ID NO: 1. As such, the recited genus of peptides consist of any two or more contiguous amino acids of SEQ ID NO: 1.
Regarding the recited genus of peptides having an amino acid sequence, which is obtained by the deletion, substitution, or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility, the recitation of “one or several amino acids” is interpreted as one or more and given the indefiniteness of “biocompatibility,” the term “biocompatibility” is interpreted as any biological activity. As such, the amino acid sequence and the function(s) of the genus of recited peptides are unlimited.
Regarding the recited genus of peptides having an amino acid sequence, which shares sequence identity equal to or higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility, given the indefiniteness of “biocompatibility,” the term “biocompatibility” is interpreted as any biological activity. As such, the function(s) of the genus of recited peptides is/are unlimited.
The genus of peptides, when treated according to the recited steps of “freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks,” “freeze-drying and pulverizing the frozen blocks,” and “sieving the pulverized blocks to obtain blocks in the form of granules,” results in granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%.
The specification discloses the actual reduction to practice of a single representative species of the recited genus of peptides that when treated according to the recited steps of “freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks,” “freeze-drying and pulverizing the frozen blocks,” and “sieving the pulverized blocks to obtain blocks in the form of granules,” result in granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90% – a polypeptide consisting of the amino acid sequence of SEQ ID NO: 1. The specification fails to disclose other representative species of the recited genus of peptides.
Regarding the level of skill and knowledge in the art of amino acid modification, MPEP 2144.08.II.A.4.(c) states, "[i]n the area of biotechnology, an exemplified species may differ from a claimed species by a conservative substitution ("the replacement in a protein of one amino acid by another, chemically similar, amino acid... [which] is generally expected to lead to either no change or only a small change in the properties of the protein." Dictionary of Biochemistry and Molecular Biology 97 (John Wiley & Sons, 2d ed. 1989)). The effect of a conservative substitution on protein function depends on the nature of the substitution and its location in the chain. Although at some locations a conservative substitution may be benign, in some proteins only one amino acid is allowed at a given position. For example, the gain or loss of even one methyl group can destabilize the structure if close packing is required in the interior of domains. James Darnell et al., Molecular Cell Biology 51 (2d ed. 1990)."
The reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached Form PTO-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 p. 7, column 1, top).
The unpredictability associated with amino acid substitution is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892), which discloses that even a substitution 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 that the recited genus of peptides encompasses species having widely variant structures and/or functions while the specification discloses only a single representative species among a widely variant genus of peptides, and given that there was a very high level of unpredictability in the art of amino acid modification at the time of the invention, the specification is considered to be insufficient to describe the recited genus of peptides. In this case, the specification at best describes a research plan for making, testing, and identifying those species that are encompassed by the recited genus of peptides, however, a plan for making the claimed invention is not sufficient to show possession at the time of filing. One of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the recited genus.
For these reasons, it is the examiner’s position that the specification fails to adequately describe the claimed invention.
Claims 1-3 are rejected under 35 U.S.C. 112(a) because the specification, while being enabling for the method of claim 1, wherein the protein comprises the amino acid sequence of SEQ ID NO: 1, does not reasonably provide enablement for the method of claim 1, wherein the protein is any of a peptide consisting of an amino acid sequence described in SEQ ID NO: 1; a peptide having an amino acid sequence, which is obtained by the deletion, substitution, or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility; or a peptide having an amino acid sequence, which shares sequence identity equal to or higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility. 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.
“The test of enablement is not whether any experimentation is necessary, but whether, if experimentation is necessary, it is undue.” In re Angstadt, 537 F.2d 498, 504, 190 USPQ 214, 219 (CCPA 1976). Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)) as follows: (A) The breadth of the claims; (B) The nature of the invention; (C) The state of the prior art; (D) The level of one of ordinary skill; (E) The level of predictability in the art; (F) The amount of direction provided by the inventor; (G) The existence of working examples; and (H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure. See MPEP § 2164.01(a). The Factors considered to be most relevant to the instant rejection are addressed in detail below.
The nature of the invention: According to the instant specification, “[a]n object of the present invention is to provide a fibrin composition, which is manufactured by a method as a substitute for a method for manufacturing platelet-rich fibrin (PRF) triggered by the activation of a coagulation factor, and a substrate for regenerative medicine using the fibrin composition. Another object of the present invention is to provide a method for manufacturing a fibrin composition, which is a substitute for a method for manufacturing PRF triggered by the activation of a coagulation factor, and a kit for being used in the method” (paragraph [0006]).
The breadth of the claims: The claims are drawn to a method for manufacturing a fibrin composition comprising blocks, fibrin and platelets, which comprises:
freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks;
freeze-drying and pulverizing the frozen blocks;
sieving the pulverized blocks to obtain blocks in the form of granules wherein the granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%;
mixing the obtained blocks and blood in a plastic container; and
subjecting the mixture of the blocks and blood to centrifugation;
wherein, an anticoagulant is not present in the fibrin composition and a platelet-rich fibrin clot is formed in the fibrin composition, and
wherein the protein is any of
a peptide consisting of an amino acid sequence described in SEQ ID NO: 1;
a peptide having an amino acid sequence, which is obtained by the deletion, substitution,
or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility; or
a peptide having an amino acid sequence, which shares sequence identity equal to or
higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility.
Regarding the recited peptide consisting of an amino acid sequence described in SEQ ID NO: 1, the recitation of “an amino acid sequence” in the phrase “an amino acid sequence described in SEQ ID NO: 1” is interpreted as any two or more contiguous amino acids of SEQ ID NO: 1. As such, the recited peptide consists of any two or more contiguous amino acids of SEQ ID NO: 1.
Regarding the recited peptide having an amino acid sequence, which is obtained by the deletion, substitution, or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility, the recitation of “one or several amino acids” is interpreted as one or more and given the indefiniteness of “biocompatibility,” the term “biocompatibility” is interpreted as any biological activity. As such, the amino acid sequence and the function(s) of the recited peptide are unlimited.
Regarding the recited peptide having an amino acid sequence, which shares sequence identity equal to or higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility, given the indefiniteness of “biocompatibility,” the term “biocompatibility” is interpreted as any biological activity. As such, the function(s) of the recited peptide is/are unlimited.
The peptide, when treated according to the recited steps of “freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks,” “freeze-drying and pulverizing the frozen blocks,” and “sieving the pulverized blocks to obtain blocks in the form of granules,” results in granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%.
The state of the prior art; The level of one of ordinary skill; and The level of predictability in the art: According to MPEP 2164.03, “…what is known in the art provides evidence as to the question of predictability.” “[I]f one skilled in the art cannot readily anticipate the effect of a change within the subject matter to which that claimed invention pertains, then there is lack of predictability in the art.” See MPEP § 2164.03.
Regarding the level of skill and knowledge in the art of amino acid modification, MPEP 2144.08.II.A.4.(c) states, "[i]n the area of biotechnology, an exemplified species may differ from a claimed species by a conservative substitution ("the replacement in a protein of one amino acid by another, chemically similar, amino acid... [which] is generally expected to lead to either no change or only a small change in the properties of the protein." Dictionary of Biochemistry and Molecular Biology 97 (John Wiley & Sons, 2d ed. 1989)). The effect of a conservative substitution on protein function depends on the nature of the substitution and its location in the chain. Although at some locations a conservative substitution may be benign, in some proteins only one amino acid is allowed at a given position. For example, the gain or loss of even one methyl group can destabilize the structure if close packing is required in the interior of domains. James Darnell et al., Molecular Cell Biology 51 (2d ed. 1990)."
The reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached Form PTO-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 p. 7, column 1, top).
The unpredictability associated with amino acid substitution is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892), which discloses that even a substitution 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).
Based on the evidence of record, one of skill in the art would recognize a high level of unpredictability in the art of amino acid modification.
The amount of direction provided by the inventor and The existence of working examples: The specification discloses a single working example of a peptide that when treated according to the recited steps of “freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks,” “freeze-drying and pulverizing the frozen blocks,” and “sieving the pulverized blocks to obtain blocks in the form of granules,” result in granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90% – a polypeptide consisting of the amino acid sequence of SEQ ID NO: 1. The specification fails to disclose other peptides that result in granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%.
The quantity of experimentation needed to make or use the invention based on the content of the disclosure: In the Federal Circuit decision of Idenix Pharmaceuticals LLC v. Gilead Sciences Inc., 941 F.3d 1149, 1156 (Fed. Cir. 2019), the court stated that “the key enablement question is whether a person of ordinary skill in the art would know, without undue experimentation, which [species] would be effective….because of the many thousands of [species] which need to be screened for…efficacy, the quantity of experimentation needed is large and weighs in favor of non-enablement.” While methods for modifying the amino acid sequence of a polypeptide were known before the effective filing date, it was not routine in the art to screen by a trial and error process for a vast number of peptides as broadly encompassed by the claims.
In view of the broad scope of the claimed genus, the lack of guidance and working examples provided in the specification, and the high degree of unpredictability, undue experimentation would be necessary for a skilled artisan to make and use the entire scope of the claimed invention. 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. 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 having the desired biological characteristics 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 § 103
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.
Claims 1-3 are rejected under 35 U.S.C. 103 as being unpatentable over Tsukioka et al. (J. Biomed. Mater. Res. B Appl. Biomater. 107:1420-1430, October, 2018; cited on the attached Form PTO-892; hereafter “Tsukioka”) in view of Oya et al. (US 2014/0378662 A1; cited on the IDS filed August 9, 2024; hereafter “Oya”).
The claims are drawn to a method for manufacturing a fibrin composition comprising blocks, fibrin and platelets, which comprises:
freezing a protein solution comprising a protein dissolved in an aqueous medium to obtain frozen blocks;
freeze-drying and pulverizing the frozen blocks;
sieving the pulverized blocks to obtain blocks in the form of granules wherein the granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%;
mixing the obtained blocks and blood in a plastic container; and
subjecting the mixture of the blocks and blood to centrifugation;
wherein, an anticoagulant is not present in the fibrin composition and a platelet-rich fibrin clot is formed in the fibrin composition, and
wherein the protein is any of
a peptide consisting of an amino acid sequence described in SEQ ID NO: 1;
a peptide having an amino acid sequence, which is obtained by the deletion, substitution,
or addition of one or several amino acids in the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility; or
a peptide having an amino acid sequence, which shares sequence identity equal to or
higher than 80% with the amino acid sequence described in SEQ ID NO: 1, and having biocompatibility.
Tsukioka teaches a biomaterial called recombinant protein and designated as “RCP” having the major characteristic of 12 RGD motifs of the alpha-1 sequence of human type I collagen present in a single molecule (p. 1420, column 1). Tsukioka teaches a particle designated as “FBG,” which is prepared from freeze-drying a solution of RCP, followed by cross-linking the RCP blocks via a heat-dependent dehydration condensation reaction and crushed into particles with an estimated porosity of 70%-95% (p. 1420, columns 1-2; p. 1421, column 1, bottom).
Tsukioka teaches platelet-rich fibrin (designated as “PRF”) is prepared by exclusion of anticoagulants and coagulation factors (p. 1421, column 1, top) and teaches mixing FBG with whole-blood samples into a plastic tube and centrifuging (paragraph bridging pp. 1421-1422).
The difference between Tsukioka and claims 1-3 is that Tsukioka does not teach sieving the crushed particles of RCP blocks to obtain blocks in the form of granules wherein the granules have such a size that the granules pass through a 1,000 μm sieve and remain on a 100 μm sieve, and a porosity of the granules is 80% to 90%.
Oya teaches a recombinant peptide designated as “CBE3” with 12 RGD sequences (see Example 1 beginning at paragraph [0136]) that is derived from a partial sequence of collagen (paragraph [0029]) including type I collagen and preferably human collagen (paragraph [0041]). Oya teaches a detailed method for preparing a tissue repair material by freezing an aqueous solution of CBE3, freeze-drying and pulverizing the resulting frozen block, and collecting a fraction of granules that passed through a sieve having openings of 710 but did not pass through a sieve having openings of 500 (see Examples 1-5 of Oya beginning at paragraph [0136]). Oya teaches cross-linking before or after the drying (paragraph [0099]) and provides exemplary methods for cross-linking including thermal cross-linking (paragraph [0100]). Oya teaches the porosity is preferably from 80% to 99.9% (paragraph [0124]).
In view of the combined teachings of Tsukioka and Oya, it would have been obvious to one of ordinary skill in the art to modify Tsukioka to prepare FBG according to Oya. One would have been motivated and would have expected success to do so because while Tsukioka generally teaches a process for preparing FBG with an estimated porosity of 70%-95% (i.e., freeze-drying a solution of RCP, followed by cross-linking the RCP blocks via a heat-dependent dehydration condensation reaction and crushed into particles), Tsukioka does not provide any specific details of the process while Oya teaches essentially the same process and porosity with detailed instructions including the step of collecting a fraction of granules that passed through a sieve having openings of 710 but did not pass through a sieve having openings of 500.
Therefore, the method of claims 1-3 would have been obvious to one of ordinary skill in the art before the effective filing date.
Citation of Relevant Prior Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. Jianpeampoolpol et al. (British Journal of Medicine and Medical Research 14:1-9, 2016; cited on the attached Form PTO-892) teaches a process for preparing platelet-rich fibrin by aliquoting blood without added anticoagulant into plastic tubes and centrifuging (paragraph bridging pp. 2-3).
Conclusion
Status of the claims:
Claims 1-3 are pending.
Claims 1-3 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656
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