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 Claims
The preliminary amendment filed 08/24/23 is acknowledged. Claim 21 is cancelled. No restriction is being imposed in this case. Claims 1-20 are pending and under examination.
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.
Claims 6, 7, 13, 16, 18-20 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.
The term “at least about” in claims 6, 7, 13, 16, and 18-20 is a relative term which renders the claim indefinite. The term “at least about” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. As such, it is unclear exactly what the lower bound for the claimed ranges are in each of the claims containing “at least about” and one of ordinary skill in the art would not be able to ascertain the scope of the claim with reasonable certainty.
The term “50% similarity with a beta sheet forming amyloid peptide” in claims 7 and 16 is indefinite because the specification does not provide specific reference sequences for beta sheet forming peptides, nor does it provide guidance on how to calculate 50% similarity. As such, one of ordinary skill in the art would not be able to ascertain the scope of the claim with reasonable certainty.
Therefore, claims 6, 7, 13, 16, and 18-20 are rejected under 35 U.S.C. 112(b) for being indefinite.
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.
Claims 1-11 and 13 are rejected under 35 U.S.C. 102a(1) as being anticipated by Dai et al.
Claims 1-7 are drawn to components for synthesizing a polymeric amyloid; claims 8-11 and 13 are drawn to methods of making a polymeric amyloid.
Dai et al. discloses linking fragments of amyloid peptide sequences (instant claims 1, 3, and 8) via a glycine-rich sequence derived from spider silk (instant claims 1, 2, 8, 10, and 17) to form block polypeptides containing 16 repeats of alternating amyloid peptides and linker sequences (instant claims 1, 6, 8, and 19) [see p. 1, abstract]. The amyloid peptide sequences are about 6-7 amino acids in length [see p. 2017, col. 1, par. 4, lines 1-7], and the spider silk linker sequence is about 28 amino acids in length [see p. 2017, col. 1, par. 3, lines 15-17], resulting in a block polypeptide of about 480 amino acids. Given an average amino acid residue weight of about 110 Da, the block polypeptide has a molecular weight of about 60 kDa (instant claim 13). Dai et al. further discloses that genes encoding these block polypeptides were inserted into plasmids, which were used to transform E. coli cells for protein expression [see p. 2016, col. 1, par. 5, lines 1-3] (instant claims 1, 5 and 8). Dai et al. discloses selecting both parallel and antiparallel amyloid peptides [see p. 2017, col. 1, par. 4, lines 1-7] (instant claims 4, 9, and 15) and discloses that these peptide sequences encode beta sheet forming amyloid [see p. 2018, fig. 3] (instant claims 7, 16, and 19). Dai et al. discloses purifying the recombinant polymeric amyloid protein [see p. 2016, col. 1, par. 2, “protein purification”] (instant claim 11) and that the expressed block polypeptides self-assemble into fibrillar structures [see p. 2017, col. 2, par. 2, lines 1-2; also see p. 2018, fig. 2]. These fibrils are characterized as comprising beta sheet rich structures [see p. 2019, col. 1, par. 2, lines 3-5; also see p. 2018, fig. 3] arising from the tandemly repeated amyloid peptide and linker sequences (instant claims 14 and 19). Furthermore, Dai et al. discloses that the fibrils exhibit a crystallinity of 32.1-34.9% [see p. 2019, col. 1, par. 2, lines 23-25] (instant claim 18) but have beta strands that are perpendicular to the fiber axis rather than parallel.
Therefore, claims 1-11 and 13 are rejected under 35 U.S.C. 102a(1).
Claim Rejections - 35 USC § 103
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.
Claims 8, 12, and 14-19 are rejected under 35 U.S.C. 103 as being unpatentable over Dai et al. in view of Meier at al.
Claims 8 and 12 are drawn to methods of making a recombinant polymeric amyloid; claims 14-19 are drawn to the specific composition of a recombinant polymeric amyloid
The disclosure of Dai et al. is discussed above and comprises the limitations of claims 15-19, which are dependent upon independent claim 14.
Dai et al. does not teach or suggest spinning the fibers as required by dependent claim 8 or that the beta sheets are parallel to the fiber axis as required by independent claim 14.
Of note, for the purposes of examination, “wherein the plurality of beta sheet crystals are aligned in parallel with a fiber axis” is interpreted to mean that the direction of beta strands are in parallel with the fiber axis, as this appears consistent with the specification [see paragraph 74].
Meier et al. teaches that the most common methods to process proteins into fibrillar materials are spinning or extruding [see p. 3454, par. 5, lines 1-2], and further discloses a specific wet-spinning method for forming fibers from amyloid protein nanofibrils (instant claim 12). Meier discloses that the resulting fibers exhibit rich beta sheet structures [see. P. 3457, col. 1, par. 1, lines 2-3]. Furthermore, Meier et al. discloses that the beta strands of beta crystals are aligned parallel to the fiber axis [see p. 3456, col. 1, par. 1, lines 8-11] (instant claim 14). Meier et al. discloses that the fibers exhibit high tensile strength and stiffness.
It would have been obvious to a person having ordinary skill in the art to combine these teachings and apply the wet spinning technique of Meier et al. to the recombinant amyloid polymers of Dai et al. to enhance the mechanical properties of the amyloid fibers (instant claim 12) by aligning beta-sheet crystal domains parallel to the fiber axis (instant claims 14-19). Additionally, a person having ordinary skill in the art would have reasonably expected that the recombinant amyloid fibrils of Dai et al. and the hen egg derived amyloid fibrils of Meier et al. would exhibit similar behavior with respect to fiber formation and alignment because both are amyloid fibrils characterized by the common crass-beta structural architecture. One would have been motivated to do so to leverage the known relationship between beta sheet alignment and mechanical performance to improve material performance.
Therefore, claims 8, 12, and 14-19 are rejected under 35 U.S.C. 103.
Claims 14 and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Dai et al. in view of Meier et al., and further in view of Bowen et al.
Claims 14 and 20 are drawn to a recombinant polymeric amyloid fiber.
The disclosure of Dai et al. and Meier et al. are discussed above and teach the limitations of independent claim 14.
Neither of these teachings disclose or suggest a polymeric amyloid fiber with beta crystals comprising 90 tandem repeats of amyloid peptides and flexible glycine linkers as required by dependent claim 20.
Bowen et al. teaches that recombinant proteins with higher molecular weight yield fibers with superior mechanical properties compared to fibers spun at lower molecular weights [see p. 3853, col. 2, lines 4-8]. Bowen et al. discloses using E. coli to generate recombinant spidroin proteins with 96 repeating units, and also generating fibers with 192 repeating units using a combination of E. coli and a technique called split intein-mediated ligation [see p. 3853, abstract] (instant claim 20).
It would have been obvious to a person having ordinary skill in the art to combine these teachings and generate recombinant polymeric amyloid comprising at least 90 block repeats because the recombinant polymeric amyloid generated by Dai et al. utilize knowledge derived from spidroin proteins, which achieves its desirable mechanical properties through repetitive beta sheet structures. Furthermore, the art recognizes that it is within the capabilities of E. coli to produce the 90 repeats, it was known that increasing repeats improves the structural characteristics of the fibers, and the largest and strongest fibers generated at the time of the invention comprised more than 90 repeats (instant claim 20).
Therefore, claims 14 and 20 are rejected under 35 U.S.C. 103
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Tirone D Johnson whose telephone number is (571)272-1256. The examiner can normally be reached M-F, 9-5 ET.
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/TIRONE D. JOHNSON/ Examiner, Art Unit 1675
/JEFFREY STUCKER/ Supervisory Patent Examiner, Art Unit 1675
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