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 .
Election/Restrictions and Claim Status
Applicant’s election without traverse of Group 1 in the reply filed on 6/20/25 is acknowledged.
Claims 11-20 are to a non-elected group.
Claims 11-20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 6/20/25.
Claims 1 and 3-10 are being examined.
Claims 1 and 3-10 are rejected.
Claim 2 is cancelled.
Priority
This application, filed 02/07/2022, is a Continuation of 16324844 , filed 02/11/2019 ,now U.S. Patent # 11242367 and having 1 RCE-type filing therein
16324844 is a National Stage entry of PCT/US2017/046659 , International Filing Date: 08/12/2017
PCT/US2017/046659 Claims Priority from Provisional Application 62467697 , filed 03/06/2017
PCT/US2017/046659 Claims Priority from Provisional Application 62407863 , filed 10/13/2016
PCT/US2017/046659 Claims Priority from Provisional Application 62374532 , filed 08/12/2016.
-Claim Interpretation
The claims limitations are given their broadest reasonable interpretation (BRI), (“[T]he ordinary and customary meaning of a claim term is the meaning that the term would have to a person of ordinary skill in the art in question at the time of the invention, i.e., as of the effective filing date of the patent application.” Phillips v. AWH Corp., 75 USPQ2d 1321, 1326 (Fed. Cir. 2005) (en banc).) The broadest reasonable interpretation of the claims must also be consistent with the interpretation that those skilled in the art would reach.” MPEP 2111, with reference to In re Cortright, 49 USPQ2d 1464, 1468. The claim limitations are given their BRI consistent with the specification, MPEP 2111, and under the BRI, words of the claim must be given their plain meaning, unless such meaning is inconsistent with the specification, MPEP 2111.01.
The specification states the following with regard to “about”:
[0043] The term “about” can refer to a variation of ±5%, ±10%, ±20%, or ±25% of the value specified. For example, “about 50” percent can in some embodiments carry a variation from 45 to 55 percent. For integer ranges, the term “about” can include one or two integers greater than and/or less than a recited integer at each end of the range. Unless indicated otherwise herein, the term “about” is intended to include values, e.g., weight percentages, proximate to the recited range that are equivalent in terms of the functionality of the individual ingredient, element, the composition, or the embodiment. The term about can also modify the end-points of a recited range as discuss above in this paragraph.
Based on the above, “about” is interpreted broadly and can extend the range of a claimed “about [value]” by up to over and less than 25% of the value. For example, the “about 60 kDa” limitation in claim 1 is interpreted to encompass a molecular weight anywhere from 45 to 75 kDa, inclusive of these endpoint values. Also as an example, claim 3’s about 39% when extended by up to over and less than 25% of the value results in a percentage value range of 29.25% to 48.75%. The same approach applies to other values in the claims.
Claim Objections
Claim 1 is objected to because of the following informalities: “HPLC” is not needed in claim 1 because there are no further references to this method in later claims for which this abbreviation could be used, and in claim 1 it is redundant. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Claims 1 and 3-10 are 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 1 now claims a fibroin-derived protein composition having a number of limitations regarding serine, glycine and alanine content, reduced or eliminated cysteine disulfide bonds, and newly added, inter alia:
the average molecular weight of the fibroin-derived protein composition is less than about 23.8 kDa as determined by High Performance Liquid Chromatography (HPLC), and
greater than about 15 kDa,
wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa, and
the composition lacks beta-sheet protein structure in the aqueous solution.
Applicant asserts support to claim 1 amendments by referring to pages in the specification, however no statement or statements in combination on those pages or elsewhere describe what is claimed. Further, in the 4/13/26 Remarks, page 6, regarding Double Patenting, reference is made to the following (which is on lines 8-12, not lines 1-5, of page 14 of the specification):
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Please note the verb “may provide” – this indicating a possibility and not definitive, and more importantly in the next sentence the adjective “typically” before “about 10-30%” (keeping in mind the interpretation of “about”), and also the parenthetical “increasing differences as molecular weights decrease”. The 10-30% range is not fixed based on the use of “typically” and the use and interpretation of “about”, yet applicant somehow selects 30% as if based on fact or evidence.
Although the examiner has identified several statements that include various amounts, percentages of molecular weights, and so forth, there is no sound technical reasoning for choosing a 30% reduction of the SDP-4’s 34 kDa average molecule weight to arrive at less than about 23.8 kDa “as determined by HPLC” (in both cases to limit the claim’s average molecular weight to “less than about” such value). This appears to be an arbitrary selection, as best understood by the examiner, and would appear to “open the door” for selecting any other fraction, at least within 0.1 to 0.3, to apply to “obtain” another HPLC average molecular weight to claim from a stated average molecular weight determined by SDS/PAGE. For any of these, lacking examples, and/or sound technical reasoning as disclosed in the application as filed, there is a lack of possession.
There also is a lack of possession for this average molecular weight less than 23.8 kDa as determined by HPLC when also considering this combined with the other limitations of claim 1, as well as limitations of dependent claims. There is no teaching of the combination of an average molecular weight less than 23.8 kDa as determined by HPLC with “and greater than 15 kDa” – the latter whether determined by SDS/PAGE or HPLC (see rejection below). Nor for other limitations in the claims is there found these in combination with an average molecular weight less than 23.8 kDa as determined by HPLC.
The “wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa” appears simply to set forth a limitation supported by the kDa ranges of SDP-4 from the table on page 43, where the average MW by SDS/PAGE is 34. Nowhere is there any indication that lower molecular weight fraction of the fibroin-derived protein composition, such as but not limited to what is below 25 kDa (the lower limit of the lowest range in that table), accounts for or results in a 30 percent reduction from the 34 kDa average MW for SDP-4 when the same composition is measured by HPLC for average MW. And there is no support from any example apart from SDP-4 that teaches an average MW less than 23.8 kDa as determined by HPLC.
Based on the above, claims 1 and 3-10 depending therefrom are rejected based on lack of possession of the claimed invention because the specification lacks adequate written description for the subject matter of what is claimed.
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 1 and 3-10 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
It is unclear whether claim 1’s “greater than about 15 kDa”, as well as the “within a range of about 20 kDa to about 60 kDa”, are determined by SDS/PAGE (as at least the latter appear to have been determined considering the results of SDP-4) or by HPLC. There is no clarity how these are determined given the amendment to “less than about 23.8 kDa as determined by” HPLC, only supposition and lack of clarity (why would these be measured by different approaches, versus why switching to HPLC is not specified for all of these?).
Claim 1, and claims 3-10 depending from claim 1, are rejected based on this lack of clarity and consequent indefiniteness.
Claim Rejections - 35 USC § 102
Response to Arguments
Applicant’s arguments, see page 5, filed 4/13/26, with respect to Claim(s) 1-10 rejected under 35 U.S.C. 102(a)(2) as being anticipated by Abdel-Naby et al. (US 2019/0117834; ‘Abdel-Naby’) have been fully considered and are persuasive. The rejection of Claim(s) 1-10 under 35 U.S.C. 102(a)(2) as being anticipated by Abdel-Naby et al., US 2019/0117834, has been withdrawn.
Claim Rejections - 35 USC § 103
Response to Arguments
Applicant’s arguments, see pages 5-6, filed 4/13/26, with respect to Claim(s) 1-10 rejected under 35 U.S.C. 103 as being obvious over Abdel-Naby et al. (US 2019/0117834; ‘Abdel-Naby’) have been fully considered and are persuasive. The rejection of Claim(s) 1-10 under 35 U.S.C. 103 has been withdrawn.
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 §§ 706.02(l)(1) - 706.02(l)(3) 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Response to Arguments
Applicant's arguments filed 4/13/26 have been fully considered but they are not persuasive.
In the 4/13/26 Remarks, page 6, regarding Double Patenting, reference is made to the following (which is on lines 8-12, not lines 1-5, of page 14 of the specification):
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Please note the verb “may provide” – this indicating a possibility and not definitive, and more importantly in the next sentence the adjective “typically” before “about 10-30%” (keeping in mind the interpretation of “about”), and also the parenthetical “increasing differences as molecular weights decrease”. The 10-30% range is not fixed based on the use of “typically” and the use and interpretation of “about”, yet applicant somehow selects 30% as if based on fact or evidence.
Although this appears to be an arbitrary selection, as best understood by the examiner, the arithmetic applied, multiplying the SDS/PAGE average molecular weight determination by 0.7 to reflect a 30% reduction, is merely representing the same composition as determined by another method to determine average molecular weight. As such, applicant is claiming the same as if claiming less than about 34 kDa as measured by SDS/PAGE. Accordingly, the bases for rejections, below, remain appropriate. (The examiner notes that the rejection over Application No. 17785392 is withdrawn based on abandonment of that application.)
Claims 1 and 3-10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 11242367 (issued parent of instant application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The following rejection is based on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE.
The 367 claims compositions are directed to a somewhat wider subgenus of fibroin-derived protein than what is instantly claimed when considering the up to +/-25% allowed variation based on “about” in the instant claims (23.8 x 1.25 = 29.75, this and greater than about 15 kDa, assuming by SDS/PAGE, establishing an outer range of 11.26 to 29.75, this overlapped by the 367’s 2 to 40 kDa range) and that the same process results in the same product, including all of its properties. The added “water” limitation in the instant claim 1 is suggested by the 367’s aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
MPEP 2144.05 recognizes that where the claimed ranges overlap with the ranges of the prior art that a prima facie case of obviousness exists. In the instant case, one would have been motivated to optimize the molecular weight range because 367 recites specific properties (enhanced stability of claim 1) associated with the compositions.
In relation to instant claims 1 and 3, given that per 367 claim 1 “39%+/−10% of the protein chains of the protein composition have a molecular weight within the range of 25 kDa to 50 kDa”, the MW limitations of instant claim 1 regarding “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” 42.8% within 25-50 kDa for 25-50 kDa is close to the instant claim 1 range without even considering 20-25 kDa and 50-60 kDa fractions, suggesting that this is close so the instant ranges would have been obvious (this not even considering the Table 1 data), and instant claim 3 would have been met by a range of embodiments encompassed by 367 claim 1, particularly those embodiments with 39%-10% having a molecular weight of 25 kDa, so claim 3 is rejected under this section.
Considering the 367 claims 1, 3 and 7, and instant claims 1 and 5, the serine content range overlaps and the lacking beta-sheet protein structure in aqueous solution is met by the 367 claims. Instant claims 1 and 3 accordingly are rejected under this section.
In relation to instant claim 4, this is rejected over 367 claims 1 and 2.
In relation to instant claim 5, this is addressed above.
In relation to instant claim 6, this is rejected over 367 claim 4.
In relation to instant claim 7, this is rejected over 367 claim 5.
In relation to instant claim 8, this is rejected over 367 claim 6.
In relation to instant claim 9, this is rejected over 367 claim 8.
In relation to instant claim 10, this is rejected over 367 claim 9.
Claims 1, 3-7, 10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 of U.S. Patent No. 11890328 (‘328’) in view of U.S. Patent No. 10953132 (‘132’).
The 328 claim 1 is directed to method of treating dry eye syndrome in a subject comprising administering an effective amount of a protein composition to an eye of the subject, thereby treating the dry eye disease, wherein the protein composition is formulated as an ophthalmic formulation comprising water; wherein the protein composition is a fibroin-derived protein composition prepared by a process comprising heating an aqueous fibroin solution at an elevated pressure, wherein: the aqueous fibroin solution comprises lithium bromide at a concentration of at least about 8M, and the aqueous fibroin solution is heated to at least about 105° C. (221° F.) under a pressure of about 10 PSI to about 20 PSI for at least about 20 minutes in the presence of the lithium bromide; to provide a protein composition comprising fibroin-derived protein wherein: the primary amino acid sequences of the fibroin-derived protein composition differ from native fibroin by at least by at least 4% with respect to the combined amino acid content of serine, glycine, and alanine, based on the combined absolute values of the differences in the content of serine, glycine, and alanine; cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains of fibroin are reduced or eliminated; the protein composition has a serine content that is reduced by greater than 25% compared to native fibroin protein; and wherein the average molecular weight of the fibroin-derived protein composition is less than about 100 kDa.
The 328 claim 6 is directed to the method of claim 1 wherein the fibroin-derived protein has an average molecular weight of less than about 60 kDa.
The 328 claim 9 is directed to the method of claim 1 wherein the fibroin-derived protein comprises between 4.5% and 7.5% serine amino acid residues, so meeting instant claim 1’s serine limitation.
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. The added “water” limitation in the instant claim 1 is suggested by the 328’s aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
Given the same greater than 25% reduction in serine per the 328 claim 1 and instant claim 1, and recognizing that this is a result of the 328 claim 1 process, the molecular weight limitations of instant claim 1 reasonably represent molecular weight results that are found in compositions made by the method of claim 1 of the 328.
Further as to the lower MW limitations of instant claim 1, the 132, directed to and claiming fibroin-derived protein also, however in its claim 1 method for treating an ocular wound, sets forth similar limitations for its silk fibroin-derived protein (SDP) fragments, and includes these having an average molecular weight between about 30 kDa and 60 kDa. For the motivation to improve the claimed subject matter of the 328, including when used for its method of treating dry eye syndrome, given that the 132 claim 1 is directed to a method for treating an ocular wound so it expected to be effective, one of ordinary skill in the art would have been motivated to further limit the molecular weight of the 328 claim 1 to conform with that of the 132 in its claim 1. The level of ordinary skill in the art is high, and there would have been a reasonable expectation of success given the claims and teachings and examples of the ‘132. With regard to embodiments of the 132 MW range meeting instant claim 1’s ““greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,”, this is based on the arithmetic relationship between number of particles and their average: to get to 30 kDa average there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW around 30 kDa, embodiments of the 132 claim 1 where the average MW is around 30 kDa would meet instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” also considering the SDS/PAGE to HPLC conversion referenced in above rejections. Accordingly instant claim 1 is rejected under this section.
In relation to instant claim 3, the MW of the 132, particularly when considering the make-up of protein fragments contributing to obtain an average molecular weight of or around 30 kDa, see analysis above, reasonably results in embodiments that fall within the MW limitations of instant claim 3, so instant claim 3 is rejected under this section.
In relation to instant claim 4, this is suggested by the low viscosity limitation of the 328 claim 7.
In relation to instant claim 5, this is met by the 328 claim 9, see also claim 12.
In relation to instant claim 6, this is rejected over 328 claim 13.
In relation to instant claim 7, this is rejected over 328 claim 15.
In relation to instant claim 10, this is rejected over 328 claim 1 (explicit as to water).
Claims 1, 3-10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 9,394,355. Although the claims at issue are not identical, they are not patentably distinct from each other.
355 claim 1 claims fibroin-derived protein compositions that possess enhanced stability in an aqueous solution wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heave and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups; the composition has a serine content that is reduced by greater than 40% compared to native fibroin protein wherein the serine content is at least about 5% and wherein the average molecular weight of the fibroin-derived protein composition is less than about 60kDa and greater than about 30kDa (claim 1). 355 recites that the composition does not gel upon ultrasonication of an aqueous solution of the protein composition at concentrations of up to 10% w/w (claim 5). 355 recites that there are specific amounts of serine, glycine and alanine (claims 6-11). 355 recites that the protein composition re-dissolves in water after being dried to a thin film (claim 12). 355 recites that the protein composition lacks beta-sheet protein structure in aqueous solution (claim 13). 355 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 14). 355 recites composition in water (claim 2).
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
Since 355 recites the average molecular weight of the fibroin-derived protein composition is less than about 60kDa and greater than about 30kDa (claim 1) one would have made such compositions (see MPEP 2131.03). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap with the ranges of the prior art that a prima facie case of obviousness exists. In the instant case, one would have been motivated to optimize the molecular weight range because 355 recites specific properties (enhanced stability of claim 1) associated with the compositions.
In relation to instant claim 1, 355 recites fibroin-derived protein compositions that possess enhanced stability in an aqueous solution wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heave and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups; the composition has a serine content that is reduced by greater than 40% compared to native fibroin protein wherein the serine content is at least about 5% and wherein the average molecular weight of the fibroin-derived protein composition is less than about 60kDa and greater than about 30kDa (claim 1). Further as to meeting the lacking beta-sheet structure in aqueous solution limitation, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these.
In relation to instant claim 3, 355 recites the average molecular weight of the fibroin-derived protein composition is less than about 60kDa and greater than about 30kDa (claim 1). When considering the make-up of protein fragments contributing to obtain an average molecular weight of or around 30 kDa, it is very reasonable that embodiments fall within the MW limitations of instant claim 3 and therefore are the basis for rejection of these claims under this section. That is, given the inclusion of the average molecular weight being as low as 30 kDa, it is very reasonable to expect that for many embodiments that fall within the 355 claim 1 where the average MW is around 30 kDa, that these embodiments would clearly meet not only instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” but also the limitations of instant claim 3. This is based on the arithmetic relationship between number of particles and their average: for example, to get to 30 kDa average there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW around 30 kDa, embodiments of the 355 claim 1 where the average MW is around 30 kDa would meet instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”, and also the limitations of instant claim 3.
In relation to claim 4, 355 recites that the composition does not gel upon ultrasonication of an aqueous solution of the protein composition at concentrations of up to 10% w/w (claim 5).
In relation to claims 5-7, 355 recites that there are specific amounts of serine, glycine and alanine (claims 6, 8 and 10).
In relation to claim 8, 355 recites that the protein composition re-dissolves in water after being dried to a thin film (claim 12).
In relation to claim 9, 355 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 14).
In relation to claim 10, 355 recites composition in water (claim 2).
Claims 1, 3-10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of U.S. Patent No. 9,907,836 (‘836’). Although the claims at issue are not identical, they are not patentably distinct from each other.
836 recites fibroin-derived protein compositions comprising water wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups; the composition has a serine content that is reduced by greater than 40% compared to native fibroin protein and wherein the average molecular weight of the fibroin-derived protein composition is less than about 60kDa (claim 1). 836 recites that the composition does not gel upon ultrasonication of an aqueous solution of the protein composition at concentrations of up to 10% w/w (claim 9). 836 recites that there are specific amounts of serine, glycine and alanine (claims 10-12). 836 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 13).
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
Since 836 recites specific serine concentrations (claim 10) one would have been motivated to make compositions with such concentrations. Since 836 recite the average molecular weight of the fibroin-derived protein composition is less than about 60kDa (claim 1) one would have made such compositions (see MPEP 2131.03). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap with the ranges of the prior art that a prima facie case of obviousness exists. In the instant case, one would have been motivated to optimize the molecular weight range because 836 recites specific properties (claim 9) associated with the compositions.
In relation to instant claim 1, 836 recites fibroin-derived protein compositions comprising water wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups; the composition has a serine content that is reduced by greater than 40% compared to native fibroin protein and wherein the average molecular weight of the fibroin-derived protein composition is less than about 60kDa (claim 1). Further, 836 recites specific serine concentrations (claim 10). Although 836 does not recite ‘possesses enhanced stability’, 836 recite or suggest the claim composition so the composition would have the features claimed (MPEP 2112.01 II). Further in this regard as to the lacking beta-sheet structure in aqueous solution limitation in instant claim 1, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these. Further, 836 recites the inclusion of a stabilizing agent (claim 3).
Further, given the inclusion of the average molecular weight being as low as 30 kDa, and with the 836 claim 14 narrowing its claim 1’s range for average molecular weight to be “about 35 kDa to about 45 kDa”, it is very reasonable to expect that for many embodiments that fall within the 836 claim 1, or claim 14, that these embodiments would clearly meet not only instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” and also the limitations of instant claim 3. This is based on the arithmetic relationship between number of particles and their average: for example, to get to an average of “about 35 kDa to about 45 kDa” there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW “about 35 kDa to about 45 kDa”, embodiments of the 836 claim 1 and claim 14 where the average MW is “about 35 kDa to about 45 kDa” reasonably would meet instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”, and also the limitations of instant claim 3.
In relation to claims 4-6, 836 recites that there are specific amounts of serine, glycine and alanine (claims 10-12).
In relation to claims 7-8, 836 recites or suggest the claimed composition so the composition would have the features claimed (MPEP 2112.01 II).
In relation to claim 9, 836 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 13).
In relation to claim 10, 836 recites fibroin-derived protein compositions comprising water (claim 1)
Claims 1, 3-10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 10,471,128 ( ‘128’). Although the claims at issue are not identical, they are not patentably distinct from each other.
128 claims fibroin-derived protein compositions that possess enhanced stability in an aqueous solution wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 4% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heave and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups (claim 11); the composition has a serine content that is reduced by greater than 25% compared to native fibroin protein and wherein the average molecular weight of the fibroin-derived protein composition is 18.75 kDa to about 100 kDa (claim 1). As to lacking beta-sheet structure in aqueous solution, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these. 128 recites that the composition does not gel upon ultrasonication of an aqueous solution of the protein composition at concentrations of up to 10% w/w (claim 4). 128 recites that there are specific amounts of serine, glycine and alanine (claims 5-10). 128 recites that the protein composition re-dissolves in water after being dried to a thin film (claim 12). 128 recites that the protein composition lacks beta-sheet protein structure in aqueous solution (claim 13). 128 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 14). 128 recites composition in water (claim 15).
Since 128 recites the average molecular weight of the fibroin-derived protein composition is 18.75 kDa to about 100 kDa (claim 1) one would have made such compositions (see MPEP 2131.03). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap with the ranges of the prior art that a prima facie case of obviousness exists. In the instant case, one would have been motivated to optimize the molecular weight range because 128 recites specific properties (enhanced stability in claim 1) associated with the compositions.
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
In relation to instant claim 1, 128 recites fibroin-derived protein compositions that possess enhanced stability in an aqueous solution wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 4% with respect to the combined amino acid content of serine, glycine and alanine; cysteine disulfide bonds between the fibroin heave and fibroin light protein chains are reduced or eliminated; a plurality of the peptide chains in the protein composition terminate in amide groups (claim 11); the composition has a serine content that is reduced by greater than 25% compared to native fibroin protein and wherein the average molecular weight of the fibroin-derived protein composition is 18.75 kDa to about 100 kDa (claim 1). Absent evidence to the contrary, given overlapping ranges and similar processing, all limitations of instant claim 1 would have been met by any of a number of compositions of the 128 within the limits of its claim 1, particularly those at the lower end of this range. This includes regarding instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” and also the limitations of instant claim 3.
In relation to instant claim 4, 128 recites that the composition does not gel upon ultrasonication of an aqueous solution of the protein composition at concentrations of up to 10% w/w (claim 4).
In relation to instant claims 4-6, 128 recites that there are specific amounts of serine, glycine and alanine (claims 5-10).
In relation to instant claim 7, 128 recites that the protein composition re-dissolves in water after being dried to a thin film (claim 12).
In relation to instant claim 8, 128 recites that the protein composition lacks beta-sheet protein structure in aqueous solution (claim 13).
In relation to instant claim 9, 128 recites that the protein composition maintains an optical absorbance in aqueous solution of less than 0.25 at 550 nm after at least five seconds of ultrasonication (claim 14).
In relation to instant claim 10, 128 recites composition in water (claim 15).
Claims 1, 3-10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11045524 (reference patent; ‘524’), in view of U.S. Patent No. 10953132 (‘132’).
The 524 claim 1 claims “A fibroin-derived protein composition that possesses enhanced stability in an aqueous solution, wherein: the primary amino acid sequences of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine, and alanine, based on the combined absolute values of the differences in the content of serine, glycine, and alanine; cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains of fibroin are reduced or eliminated; the protein composition has a serine content that is reduced by greater than 25% compared to native fibroin protein, and the protein composition comprises between 4.5% and 7.5% serine amino acid residues; wherein the average molecular weight of the fibroin-derived protein composition is less than about 100 kDa; and wherein the protein composition has an aqueous viscosity of less than 4 cP as a 10% w/w solution in water” but does not claim a lower limit or range of the average molecular weight of the fibroin-derived protein composition. The 524 claim 11 meets this same limitation in instant claim 1.
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
The 132, directed to and claiming fibroin-derived protein also, however in its claim 1 method for treating an ocular wound, sets forth similar limitations for its silk fibroin-derived protein (SDP) fragments, and includes these having an average molecular weight between about 30 kDa and 60 kDa. For the purposes of improving the claimed subject matter of the 524, including when it is used in an ophthalmic formulation per its claim 14, it would have been obvious to one of ordinary skill in the art to further limit the molecular weight to conform with that of the 132 in its claim 1, at least given that the latter was used for treating an ocular wound. As to lacking beta-sheet structure in aqueous solution, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference, and including the narrower MW range of the 132, based on having the same or similarly modified amino acid composition and process treatments to obtain these.
The level of ordinary skill in the art is high, and there would have been a reasonable expectation of success given the claims and teachings and examples of the ‘132. Accordingly the 524 instant claim 1 is rejected under this section.
In relation to instant claim 3, the MW of the 132, particularly when considering the make-up of protein fragments contributing to obtain an average molecular weight of or around 30 kDa, reasonably results in embodiments that fall within the MW limitations of instant claim 3. That is, given the inclusion of the average molecular weight being as low as 30 kDa, it is very reasonable to expect that for many embodiments that fall within the 132 claim 1 where the average MW is around 30 kDa, that these embodiments would clearly meet instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” and also the limitations of instant claim 3. This is based on the arithmetic relationship between number of particles and their average: to get to 30 kDa average (or thereabouts) there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW around 30 kDa, embodiments of the 132 claim 1 where the average MW is around 30 kDa would meet instant claim 1’s “greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa,” and also the limitations of instant claim 3.
In relation to instant claim 4, this is rejected over 524 claim 4.
In relation to instant claim 5, this is met by the 524 claim 1 range for serine.
In relation to instant claim 6, this is rejected over 524 claim 5.
In relation to instant claim 7, this is rejected over 524 claim 7.
In relation to instant claim 8, this is rejected over 524 claim 10.
In relation to instant claim 9, this is rejected over 524 claim 12.
In relation to instant claim 10, this is rejected over 524 claim 1 (aqueous solution), and also confirmed by claim 2 (explicit as to water).
Claims 1-3, 5-7, 10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-12 of U.S. Patent No. 10953132 (reference patent; ‘132’). Although the claims at issue are not identical, they are not patentably distinct from each other.
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
The 132, directed to and claiming fibroin-derived protein, in its claim 1 method for treating an ocular wound, sets forth limitations the same as or similar to instant claim 1 (see below), and for its silk fibroin-derived protein (SDP) fragments includes these having an average molecular weight between about 30 kDa and 60 kDa. This range overlaps instant claim 1’s less than about 23.8 kDa and greater than about 15 kDa when considering the above SDS/PAGE to HPLC conversion, and given the inclusion of the average molecular weight being as low as 30 kDa (or lower when considering the range of “about” defined in its para 19), it is very reasonable to expect that for many embodiments that fall within the 132 claim 1 where the average MW is around 30 kDa, that these embodiments would clearly meet instant claim 1’s “wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”. This is based on the arithmetic relationship between number of particles and their average: for example, to get to 30 kDa average there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW around 30 kDa, embodiments of the 132 claim 1 where the average MW is around 30 kDa would meet instant claim 1’s “wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”. The same analysis applies to the limitations of claims 3. As to lacking beta-sheet structure in aqueous solution, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these.
Further, 132 recites fibroin-derived protein compositions (claim 1) that possess enhanced stability in an aqueous solution (claim 3) wherein the primary amino acid sequence of the fibroin-derived protein composition differ from native fibroin by at least 4% with respect to the combined amino acid content of serine, glycine and alanine (claim 1); cysteine disulfide bonds between the fibroin heave and fibroin light protein chains are reduced or eliminated (claim 2); a plurality of the peptide chains in the protein composition terminate in amide groups (claim 1); the composition has a serine content that is reduced by greater than 40% compared to native fibroin protein wherein the serine content is at least about 5% (claim 1) and wherein the average molecular weight of the fibroin-derived protein composition is between about 30kDa and 60kDa (as discussed above).
Since 132 recites compositions that are used in a method one would have been motivated to make the compositions. Since 132 recites the average molecular weight of the fibroin-derived protein composition is between about 30 kDa and 60 kDa (claim 8) one would have made such compositions (see MPEP 2131.03). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap with the ranges of the prior art that a prima facie case of obviousness exists. In the instant case, one would have been motivated to optimize the molecular weight range because 132 recites specific uses of the compositions and specific properties (claims 1-3). Further, since 132 recites serine, glycine and alanine in the compositions (claim 1) one would have been motivated to optimize the amounts.
Based on the above, instant claim 1 is rejected under this section.
Further in relation to claim 3, in addition to the above reasoning applied to claim 1, and the Claim Interpretation regarding “about”, 132 recites or suggests the claimed composition so the composition would have the features claimed (MPEP 2112.01 II).
In relation to claims 5-7, 132 recites serine, glycine and alanine in the compositions (claim 1) so one would have been motivated to optimize the amounts, and alternatively 132 claim 1 recites or suggests the claimed composition so the composition would have the features claimed (MPEP 2112.01 II).
In relation to claim 10, 132 recites aqueous compositions (claim 12).
Further as to instant claim 1’s limitations/properties not specified in the 132 claims, the Patent Office does not have the facilities to test the composition claimed in the 132, and given that the 132 and the instant application are directed to preparing the fibroin-derived proteins/fragments using the same processes there is a reasonable bases that the claim limitations are met. Thus the claim limitations not explicitly recited in the 132 claims are met absent evidence to the contrary (see MPEP 2112 V and MPEP 2112.01 II).
Claims 1, 3-7, 10 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, 6, 8 of U.S. Patent No. 12350321 (‘321’) in view of U.S. Patent No. 10953132 (‘132’).
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
The 321 claim 1 is directed to fibroin-derived protein composition prepared by a process comprising heating an aqueous fibroin solution at an elevated pressure, wherein: the aqueous fibroin solution comprises lithium bromide at a concentration of at least about 8M, and the aqueous fibroin solution is heated to at least about 105° C. (221° F.) under a pressure of about 10 PSI to about 20 PSI for at least about 20 minutes in the presence of the lithium bromide; to provide a protein composition comprising fibroin-derived protein wherein: the primary amino acid sequences of the fibroin-derived protein composition differ from native fibroin by at least 6% with respect to the combined amino acid content of serine, glycine, and alanine, based on the combined absolute values of the differences in the content of serine, glycine, and alanine; cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains of fibroin are reduced or eliminated; the protein composition has a serine content that is reduced by greater than 25% compared to native fibroin protein, wherein the protein composition comprises between 4.5% and 7.5% serine amino acids residues; wherein the average molecular weight of the fibroin-derived protein composition is less than about 100 kDa; and wherein the protein composition has an aqueous viscosity of less than 5 cP as a 10% w/w solution in water.
The 321 claim 3 is directed to the method of claim 1 wherein the fibroin-derived protein has an average molecular weight of less than about 60 kDa. This necessarily includes lower molecule weight averages, including those around 30 kDa, those around 40 kDa, and there between.
As to the lower MW limitation of instant claim 1, the 132, directed to and claiming fibroin-derived protein also, however in its claim 1 method for treating an ocular wound, sets forth similar limitations for its silk fibroin-derived protein (SDP) fragments, and includes these having an average molecular weight between about 30 kDa and 60 kDa. For the purposes of improving the claimed subject matter of the 321, it would have been obvious to one of ordinary skill in the art to further limit the molecular weight to conform with that of the 132 in its claim 1. The level of ordinary skill in the art is high, and there would have been a reasonable expectation of success given the claims and teachings and examples of the 132. With regard to embodiments of the 132 MW range meeting instant claim 1’s “wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”, this is based on the arithmetic relationship between number of particles and their average: for example to get to 30 kDa average there cannot be too many very high MW protein chains to be included into the averaging, these being balanced against smaller particles that each contribute less to the total weight. Absent evidence to the contrary, based on the need to balance weights of individual SDP fragments to meet an average MW around 30 kDa, embodiments of the 132 claim 1 where the average MW is around 30 kDa would meet instant claim 1’s “wherein greater than 50% of the protein chains of the protein composition have a molecular weight within a range of about 20 kDa to about 60 kDa”. As to lacking beta-sheet structure in aqueous solution, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these.
Accordingly instant claim 1 is rejected under this section.
In relation to instant claims 2 and 3, the MW range of the 132 claim 1, particularly when considering the make-up of protein fragments contributing to obtain an average molecular weight of or around 30 kDa, reasonably results in embodiments that fall within the MW limitations of instant claims 2 and 3, so instant claims 2 and 3 are rejected under this section.
In relation to instant claim 4, this is suggested by the low viscosity limitation of the 321 claim 4.
In relation to instant claim 5, this is met by the 321 claim 1 range of between 4.5 and 7.5 percent for serine.
In relation to instant claim 6, this is rejected over 321 claim 6.
In relation to instant claim 7, this is rejected over 321 claim 8.
In relation to instant claim 10, this is rejected over 321 claim 1 (explicit as to water).
Claims 1, 3, 5-7, 10 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1, 2, 4, 9, 10, 16 of copending Application No. 17377159 (‘159’).
This rejection is based at least in part on the reasoning that the instant limitation including “less than about 23.8 kDa as determined by High Performance Liquid Chromatography” corresponds to “less than about 39 kDa” when a fibroin-derived protein composition is measured, as done in the application as filed, by SDS/PAGE. Also, the added “water” limitation in the instant claim 1 is suggested by the instant reference claims’ aqueous solution reference, and any lack of beta-sheet protein structure would occur in the common aqueous solution for the compositions that fall within both claims based on the same compositions necessarily possessing the same properties.
Although the claims at issue are not identical, they are not patentably distinct from each other because the 159 claims 1, 2, 4 and 16 recite claim limitations that substantially overlap instant claim 1’s MW range (whether determined by SDS/PAGE or as modified by applicant’s conversion to HPLC) and at least based on the lower range average MW of 159 claim 1, 15-22 kDa, reasonably meet instant claim 1’s limitation of greater than 50% of the protein chains having a MW within a range of about 20 kDa to about 60 kDa. These claims also meet the 4% difference limitation, the reduced serine limitation and amount (see claim 16). As to lacking beta-sheet structure in aqueous solution, and presence of buffering agents in the 159 claim 1, the latter is suggested by reference to aqueous solution and as to the former, absent evidence to the contrary this is an inherent property of the composition set forth in the referred to claims of the cited reference based on having the same or similarly modified amino acid composition and process treatments to obtain these.
Accordingly, instant claim 1 is rejected over the 159 claims 1, 4 and 16 under this section.
In relation to instant claim 3, the MW of 159 claim 1, particularly when considering the make-up of protein fragments contributing to obtain an average molecular weight of or around 15 or 22 kDa, reasonably results in embodiments that fall within the MW limitations of instant claim 3, so instant claim 3 is rejected under this section.
In relation to instant claim 5, this is met by the 159 claim 2 serine limitation.
In relation to instant claim 6, this is rejected over 159 claim 2 glycine limitation.
In relation to instant claim 7, this is rejected over 159 claim 2 alanine.
In relation to instant claim 10, this is rejected over 159 claims 1, 9, 10 and 16, which refer to buffers and millimolar amounts, suggesting the presence of water.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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.
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/JOSEPH FISCHER/Primary Examiner, Art Unit 1658
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