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
Applicants’ election without traverse of Group I (i.e., claims 1-13 drawn to a synthetic peptide) in the reply filed on 01/23/2026 is acknowledged. Applicants’ election of SEQ ID NO: 6 (i.e., Species A), without traverse, in the reply filed on 01/23/2026 is also acknowledged.
Claims 14-19 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, and claims 3-4 and 6-12 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species; there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 01/23/2026.
Upon extensive search and examination, it has been determined that the elected species (i.e., SEQ ID NO: 6), is free of the prior art. Accordingly, for purposes of compact prosecution, the election of species is modified only to the extent of examining additional species (i.e., SEQ ID NOs: 12 and 13). Otherwise the election of species requirement is still retained.
Priority
The present application also claims status as a 371 (National Stage) of PCT/US2021/057495 filed November 1st 2021, and claims the benefit under 35 U.S.C 119 (e) to U.S. Provisional Application No. 63/108,762 filed November 2nd 2020. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C 119 (e) or under 35 U.S.C 120, 121, or 365 (c ) is acknowledged.
Sequence Interpretation
Regarding claim 1, the Examiner is interpreting the scope of a synthetic peptide as requiring at least 95% sequence identity to SEQ ID NO: 6 (Applicants’ elected species), with any N-/C-terminal additions. Since SEQ ID NO: 6 is 15 amino acids in length, a sequence that is at least about 95% identical would encompass up to 1 modification including any insertions, substitutions, deletions, etc.
Regarding claim 2, the Examiner is interpreting the scope of the synthetic peptide as requiring 100% identity to SEQ ID NO: 6 (Applicants’ elected species), with any N-/C-terminal additions.
Regarding claims 1 and 5, the Examiner is interpreting the scope of a synthetic peptide as requiring at least 95% sequence identity to SEQ ID NO: 6 (Applicants’ elected species), with any N-/C-terminal additions. Since SEQ ID NO: 6 is 15 amino acids in length, a sequence that is at least about 95% identical would encompass up to 1 modification including any insertions, substitutions, deletions, etc.
Response to Arguments
1. Applicants’ arguments, see Remarks, filed 05/22/202, with respect to the claim objections have been fully considered and are persuasive. The objections to claims 1, 2 and 5 has been withdrawn.
2. Applicants’ arguments, see Remarks, filed 05/22/202, with respect to the 35 U.S.C. 102 rejection have been fully considered but are not are persuasive. The 35 U.S.C. 102 rejection to claims 1, 5 and 13 has been maintained.
3. Applicants’ arguments, see Remarks, filed 05/22/202, with respect to the nonstatutory double patenting rejections have been fully considered but are not persuasive. The NSDP rejections have been maintained.
New Rejections
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.
1. Claims 1 and 5 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.
Claims 1 and 5 recite the phrase “at least about 95% sequence identity” which conflates qualitative and quantitative language, and is therefore indefinite because it is unknown if 80%, 85%, 90%, 94%, 94.9%, etc. read upon the claim scope or not, since such numbers are “about 95%”, but are not “at least” 95%. For purposes of applying prior art, the phrase “at least about 95%” is interpreted as nested limitations, wherein “about 95%” includes “within an order of magnitude” of 95% (see, e.g., Spec. filed 5/01/2023 at pg. 11, last paragraph), which is 9.5%, and therefore the phrase “at least about 95%” is understood to mean “at least 9.5%” as in 9.5% or more.
Additionally, the phrase “at least about 95% sequence identity” which recites “about”, which has been defined in multiple, distinct ways on record, which therefore renders the claim scope indefinite. Specifically, “about” is defined in multiple distinct ways including as “within an acceptable standard deviation”, “±20%”, “±10%”, “±5%”, “±1%”, “within an order of magnitude”, or “preferably within 2-fold” (see, e.g., Spec. filed 5/01/2023 at pg. 11, last paragraph). Accordingly, the claim scope materially changes depending upon the selected interpretation because “about 95% sequence identity” could be interpreted, consistent with the specification, to mean:
at least 9.5% sequence identity (i.e., within an order of magnitude of 95%);
at least 47.5% sequence identity (i.e., within 2-fold of 95%);
at least 76% sequence identity (i.e., ±20% of 95%);
at least 85.5% sequence identity (i.e., ±10% of 95%);
at least 90.25% sequence identity (i.e., ±5% of 95%); or
at least 94.05% sequence identity (i.e., ±1% of 95%).
This is pertinent because SEQ ID NOs: 6-13 are 15-mers, and 15-mers can only exhibit the following values of sequence identity over the full-length of the sequence: 100% (15/15); 93.33% (14/15); 86.67% (13/15); 80% (12/15); 73.33% (11/15); 66.66% (10/15); 60% (9/15); 53.33% (8/15); 46.67% (7/15); 40% (6/15); 33.33% (5/15); 26.67% (4/15); 20% (3/15); 13.33% (2/15); and 6.67% (1/15). Accordingly, the specific meaning and definition of “about” utilized materially alters the pending claim scope such that the claims may include or exclude sequences sharing 14/15 to 2/15 residues in common with any one of instant SEQ ID NOs: 6-13.
Close prior art exists as evidenced by the prior art applied under 35 USC 102 and 103, as set forth below. Therefore, for purposes of applying prior art, the phrase “at least about 95%” is interpreted as nested limitations, wherein “about 95%” includes “within an order of magnitude” of 95% (see, e.g., Spec. filed 5/01/2023 at pg. 11, last paragraph), which is 9.5%, and therefore the phrase “at least about 95%” is understood to mean “at least 9.5%”. This is reasonable, because it simply reflects the broadest definition of “about” set forth on record in the instant disclosure (see, e.g., Spec. filed 5/01/2023 at pg. 11, last paragraph).
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
2. Claims 1-2, 5 and 13 are rejected under 35 U.S.C. 103 as being unpatentable over US 10,005,818 B2 Date of Patent Jun. 26, 2018 (cited in the IDS filed on 05/06/2024) (herein after “ Krishna et al.”) in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”).
Regarding claims 1-2 and 5, Krishna et al. claim a synthetic peptide comprising at least about 90% sequence identity to the amino acid sequence of SEQ ID NO: 3-47 (see column 79, claim 1). As discussed in the “Sequence interpretation” section above, a sequence that is about 95% identical to instant SEQ ID NO: 6 encompasses up to one modification. Krishna’s SEQ ID NO: 11 is 15 residues in length and includes sarcosine at position 8 (see column 61, last entry).
The difference between Krishna’s SEQ ID NO: 11 and instant SEQ ID NO: 6 is that the amino acid at position 3 (i.e., Leu) is not a D-amino acid (e.g., D-Leu).
Simon et al. teach that a D-scan is powerful new strategy for studying how the stereochemistry of amino acids affects the structure and function of proteins (see pg. 12099, Abstract). Simon et al. add that using D-amino acids in a protein would allow access to a broader folding and structural space; that substitution of D-amino acids for glycine in a favorable conformation can improve thermal stability; and that targeted insertions elsewhere can improve stability toward protease, as reported by other sources cited by Simon et al (see pg. 12099, left column, last paragraph). Furthermore, that D-scans of several bioactive peptides have shown them to be tolerant of D-amino acid substitutions with some constructs having enhanced biological properties (see pg. 12099, right column, first paragraph). Like an alanine scan, which is used to determine which side chains are important for function and folding; a “D-scan” identifies the important chiral centers for folding and activity in a small peptide (see pg. 12099, right column, last paragraph). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see pg. 12110, columns I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at Introduction; and pg. 12110 at col I-II).
As such, an ordinary skilled artisan would have been motivated with reasonable expectation of success before the effective filing date of the claimed invention, to arrive at the instantly claimed synthetic peptide comprising at least 95% sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs: 6-13, in view of the prior art.
One of ordinary skilled in the art would have been motivated to do so because it was known that a D-scan is powerful strategy for studying how the stereochemistry of amino acids affects the structure and function of proteins; because using D-amino acids in a protein would allow access to a broader folding and structural space; and because targeted D-amino acid insertions can improve stability. One of ordinary skilled in the art would have had a reasonable expectation of success given that a D-scan helps identify the important chiral centers for folding and activity in a small peptide. Therefore, the instantly claimed invention is an obvious result of applying and using the known technique and methodology of Simon et al. (i.e., a D-scan) to the known sequence of Krishna (i.e., SEQ ID NO: 11). As such, the teachings of Simon et al. when combined with the teachings of Krishna would support the claimed invention by constituting some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention, and/or the use of a known technique to improve similar devices (methods, or products) in the same way, pursuant to KSR.
Regarding claim 13, Krishna et al. claim a pharmaceutical composition comprising a therapeutically effective amount of the synthetic peptide of claim 1, and at least one pharmaceutically acceptable carrier, diluent, or excipient (see column 79, claim 5, lines 45-48). Therefore, Krishna et al.’s invention reads on the instantly claimed pharmaceutical composition as recited in instant claim 13.
From the teachings of the references, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention.
Maintained/Modified Rejections
Claim Rejections - 35 USC § 102
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.
3. Claims 1, 5 and 13 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by US 10,005,818 B2 Date of Patent Jun. 26, 2018 (cited in the IDS filed on 05/06/2024) (herein after “ Krishna et al.”), as evidenced by GenCore Sequence Alignment.
For claims 1 and 5, Krishna et al. disclose a synthetic peptide comprising at least about 90% sequence identity to the amino acid sequence of SEQ ID NO: 3-47 (see column 79, claim 1, lines 33-35). Kishna et al. also disclose SEQ ID NO: 11, which is 15 residues in length and includes sarcosine at position 8; therefore the amino acid residue at position 8 is sarcosine (see column 61, last entry).
As evidenced by GenCore, instant SEQ ID NO:6 (i.e., Applicants’ elected species) is 98.6% identical to Krishna et al.’s SEQ ID NO: 11 (see GenCore Sequence Alignment). As such, the disclosure of Krishna et al. anticipates the instantly claimed synthetic peptide comprising at least about 95% sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NOs: 6-13, as recited in instant claims 1; wherein the synthetic peptide of claim 1 comprises an amino acid sequence selected from the group consisting of SEQ ID NOs: 6-13, as recited in instant claim 2; and also anticipates the synthetic peptide of claim 1 consisting of an amino acid sequence comprising at least about 95% sequence identity to SEQ ID NO: 6, as recited in instant claim 5.
For claim 13, Krishna et al. claim a pharmaceutical composition comprising a therapeutically effective amount of the synthetic peptide of claim 1, and at least one pharmaceutically acceptable carrier, diluent, or excipient (see column 79, claim 5, lines 45-48). Therefore, Krishna et al.’s disclosure anticipate the claim limitations recited in instant claim 13.
Accordingly, instant claims 1, 5 and 13 are anticipated by the disclosure of Krishna et al.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
4. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 and 5-13 of U.S. Patent No. 10,005,818 B2 (here in after “Krishna et al.”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”).
Regarding instant claims 1-2, 5 and 13, Krishna et al. claims:
SEQ ID NO: 11 and pharmaceutical formulations comprising SEQ ID NO: 11, and methods utilizing SEQ ID NO: 11 (see, e.g., Krishna at claims 1-2, 5-13). This is pertinent because SEQ ID NO: 11 of US’818 is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., Krishna et al. at SEQ ID NO: 11).
However, Krishna et al. do not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of Krishna’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
5. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 and 17-19 of U.S. Patent No. 11,135,272 B2 Date of Patent: Oct. 5, 2021 (here in after “US’272”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding instant claims 1-2, 5 and 13, US ‘272 claims:
Methods of administering “PIC1” to a subject, which necessitates that “PIC1” is in a pharmaceutically acceptable form (see, e.g., US’272 at claims 1-13 and 17-19). The structure of a “PIC1” is not explicitly recited in the claims, but it is reasonably inferred that this term refers to a genus of structures in view of claims 14-16 of US’272. Per MPEP § 804(II)(B)(1), it is permissible to use the specification as a dictionary to learn the meaning of a term in a claim (see, e.g., MPEP § 804(II)(B)(1)), and in US’272 the term is reasonably inferred and understood to encompass SEQ ID NO: 9 (see, e.g., US’272 at SEQ ID NO:9, col. 8 at lines 15-60 and Table 1 disclosing “examples of PIC1 and PIC1 variants”). This is pertinent because SEQ ID NO: 9 of US’272 is understood to have the following structure: IALILEP(Sar)CCQERAA, which corresponds to instant SEQ ID NO: 6 (i.e., IALILEPXCCQERAA, wherein X is Sar).
However, US ‘272 does not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of US ‘272’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
6. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3-4 and 7 of U.S. Patent No. 10,933,116 B2 Date of Patent: Mar. 2, 2021 (here in after “US ‘116”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding instant claims 1-2, 5 and 13, US ‘116 claims:
Methods that require pharmaceutical formulations comprising SEQ ID NO: 11 (see, e.g., US’116 at SEQ ID NO:11, claims 1, 3-4, and 7). This is pertinent because SEQ ID NO: 11 of the primary reference is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., US’116 at SEQ ID NO: 11).
However, US ‘116 does not does not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of US ‘116’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
7. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4 and 9 of U.S. Patent No. 10,947,279 Date of Patent: Mar. 16, 2021 (here in after “US ‘279”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding instant claims 1-2, 5 and 13, US ‘279 claims:
A peptide comprising the amino acid sequence of any of SEQ ID NOs: 5, 6, 7, 8, 11, 12, and 31 (see US ‘279, column 79, claim 1); a pharmaceutical composition comprising a therapeutically effective amount of the peptide of claim 1 and at least one pharmaceutically acceptable carrier, diluent, or excipient (see US ‘279, column 79, claim 2); the peptide of claim 1 comprising the amino acid sequence set forth in SEQ ID NO: 11 (see US ‘279, column 79, claim 3); a pharmaceutical composition comprising a therapeutically effective amount of the peptide of claim 3 and at least one pharmaceutically acceptable carrier, diluent, or excipient (see US ‘279, column 79, claim 4); and the peptide of claim 1 comprising the amino acid sequence of SEQ ID NO: 11 (see US ‘279, column 79, claim 9).
However, US ‘279 does not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of US ‘279’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
8. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 8 of U.S. Patent No. 11, 814,414 Date of Patent: Nov. 14, 2023 (here in after “US ‘414”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding instant claims 1-2, 5 and 13, US ‘414 claims:
Pharmaceutical formulations comprising SEQ ID NO: 11 (see, e.g., US’414 at SEQ ID NO:11, claims 1-3 and 8). This is pertinent because SEQ ID NO: 11 of the primary reference is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., US’414 at SEQ ID NO: 11).
However, US ‘414 does not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of US ‘414’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
9. Claims 1-2, 5 and 13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5 and 10 of U.S. Patent No. 12,297,235 Date of Patent: May 13, 2025 (here in after “US ‘235”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding instant claims 1-2, 5 and 13, US ‘235 claims:
Methods utilizing pharmaceutical formulations comprising SEQ ID NO: 11 (see, e.g., US’235 at SEQ ID NO:11, claims 1-3 and 8). This is pertinent because SEQ ID NO: 11 of the primary reference is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., US’235 at SEQ ID NO: 11).
However, US ‘235 does not does not expressly teach that the sequence encompasses a D-amino acid, as depicted in the sequence listing of the instant application, for instant SEQ ID NO: 6.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of US ‘235’s invention because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Accordingly, instant claims 1-2, 5 and 13 are rejected.
10. Claims 1-2, 5 and 13 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 5 of Copending Application No. 19/182,023 (PGPub US20260132170A1), claim set filed on 04/17/2025 (here in after “023”), as evidenced by GenCore Sequence Alignment of instant SEQ ID NO: 6 v ‘023’s SEQ ID NO: 11, in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”).
Regarding instant claims 1-2 and 5, ‘023 claims:
A synthetic peptide comprising at least about 90% sequence identity to the amino acid sequence of SEQ ID NO: 3-47 (see ‘023, claim 1). As evidenced by the GenCore sequence alignment, instant SEQ ID NO: 6 is 98.6% percent identical to ‘023’s SEQ ID NO: 11.
However, SEQ ID NO: 11 in Copending App ‘023 does not encompass a D-amino acid at position 3.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of SEQ ID NO: 11 in Copending App ‘023 because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Regarding instant claim 13, ‘023 claims:
A pharmaceutical composition comprising a therapeutically effective amount of the synthetic peptide of claim 1 and at least one pharmaceutically acceptable carrier, diluent, or excipient (see ‘023, claim 5).
Although the claims are issue are not identical, they are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
11. Claims 1-2, 5 and 13 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-23 of Copending Application No. 18/035,846, (PGPub US20230414506A1) claim set filed on 02/18/2026 (here in after “846”), in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding claims 1-2, 5 and 13, Copending App ‘846 claims:
A pharmaceutical formulations comprising SEQ ID NO: 3 (see, e.g., App’846 at SEQ ID NO:3, claims 1-23). This is pertinent because SEQ ID NO: 3 of the primary reference is PA-I8Sar, which is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., App’846 at SEQ ID NO: 3).
However, SEQ ID NO: 3 in Copending App ‘846 does not encompass a D-amino acid at position 3.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of SEQ ID NO: 3 in Copending App ‘846 because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Although the claims are issue are not identical, they are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
12. Claims 1-2, 5 and 13 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 2-18 of Copending Application No. 18/288,274 (PG Pub US20240209036A1), claim set filed on 10/25/2023 1 of 2 (here in after “274”) in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding claims 1-2, 5 and 13, Copending App ‘274 claims:
A pharmaceutical formulations comprising SEQ ID NO: 3 (see, e.g., App’274 at SEQ ID NO:3, claims 2-18). This is pertinent because SEQ ID NO: 3 of the primary reference is PA-I8Sar, which is understood to have the following structure: IALILEP(Sar)CCQERAA (see, e.g., App’846 at SEQ ID NO: 3).
However, SEQ ID NO: 3 in Copending App ‘274 does not encompass a D-amino acid at position 3.
Simon et al. pertain to D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Accordingly, the present claims are directed to obvious variants of SEQ ID NO: 3 in Copending App ‘274 because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Although the claims are issue are not identical, they are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
13. Claims 1-2, 5 and 13 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 10 and 18 of Copending Application No. 18/034,731 (PG Pub US20230272012A1), claim set filed on 01/23/2026 (here in after “371”) in view of Simon et al., Journal of the American Chemical Society 2016, vol. 138, issue 37, pp. 12099-12111 (herein after “Simon et al.”). This is a new rejection.
Regarding claims 1-2, 5 and 13, Copending App ‘371 claims:
Pharmaceutical formulations comprising related compounds that are highly similar to the claimed sequences (compare instant claims 1-2, 5 and 13 with copending claims 1-2, 10 and 18 of App’731).
Both copending claim sets are directed to derivatives and variants of PA-I8Sar (RLS-0088) and PA-C9Sar (RLS-0089) sequences, but the derivatives differ with respect to the exact placement of modifications relative to these base sequences (compare instant Spec. filed 5/01/2023 at Table 1, pp. 22-23). Nothing that the PA and RLS numbers are mostly consecutive, but then skip PA-0122, RLS-0122, IAdLILEP(Sar)CCQERAA which corresponds to instant SEQ ID NO: 6 as claimed.
Accordingly, the issue is whether or not the copending claims are patently distinct from one another under an obviousness rationale (see, e.g., MPEP § 804(II)(B)(2)-(3)).
Upon review of the pending claim scope and copending application, App’731 at SEQ ID NO: 13 (i.e., PA-0121, RLS-0121, IdALILEP(Sar)CCQERAA); it is noted that both sequences share the same core structure (i.e., IALILEP(Sar)CCQERAA) but the position of the D-amino acid varies.
Accordingly, the relevant issue is whether or not copending claims directed to D-amino acid substitution variants of the same exact base sequence, render other unclaimed D-amino acid substitutions of the same exact base sequence obvious or otherwise patentably indistinct.
Simon pertains D-amino acid substitutions in polypeptides, and Simon explains that a “D-scan” was known and routine in the prior art at least circa 2016 (see, e.g., Simon at title, abs). A “D-scan” is analogous to an alanine scan, but wherein D-amino acids are substituted at each position of a short polypeptide (see, e.g., Simon at title, abs, 12099 at col I-II at § Introduction, 12099-12100 at bridging ¶, 12100 at Fig. 1). The D-scan methodology provides known benefits, including the identification of critical stereocenters required for activity and identification of residues amenable to D-amino acid substitutions without abrogating functionality (see, e.g., Simon at title, abs, 12109 at col II at § Conclusion, 12110 at col I-II). Simon explains that some D-amino acid substitutions may be harmful by abolishing function or impacting folding (see, e.g., Simon at 12110 at col I-II), but that D-amino acid insertions can also desirably and predictably stabilize proteins against proteolysis (see, e.g., Simon at 12099 at § Introduction; 12110 at col I-II). Accordingly, performing a “D-scan” by converting each amino acid within a short polypeptide into a D-amino acid, one at a time, is a known method having known benefits, which would be routine to perform in order to identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide.
Under an obviousness analysis (see, e.g., MPEP § 804(II)(B)(3)), it is noted that the scope and content of the patent claim relative to the application claims at issue have been discussed above (see, e.g., MPEP § 804(II)(B)(3)(A)), and that the differences are that the instant claims attempt to claim a different D-amino acid substituted variants of the same common base sequences (e.g., PA-I8Sar (RLS-0088). Accordingly, the present claims are directed to obvious variants of the copending claims because an artisan would readily appreciate that other D-amino acid variants of the same exact base sequence (i.e., the ones instantly claimed) could predictably, routinely, and desirably be made via a D-scan methodology exactly as taught and suggested by Simon applied to the D-amino acid variants claimed by the primary reference, wherein the creation of such D-amino acid variants would predictably and expectedly identify critical stereocenters and positions amenable to D-amino acid substitutions, wherein D-amino acid substitutions at positions amenable to such substitutions, would predictably increase protease resistance and stability of the peptide (see, e.g., MPEP §§ 2143(I)(B), (C), (D), (F), (G), 2144.09; see, e.g., MPEP § 804(II)(B)(3)(B)).
Although the claims are issue are not identical, they are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicant's arguments filed 05/22/2026 with respect to the 35 U.S.C 102 rejection to claims 1, 5 and 13, have been fully considered but they are not persuasive.
In response to Applicants’ argument, i.e., the cited prior art does not anticipate the claimed invention because the prior art fails to teach or disclose that D-enantiomers of certain amino acids can be substituted in SEQ ID NOs: 3-47 taught in Krishna, or that stapled modifications of SEQ ID NOs: 3-47 can be made (see Remarks, filed 05/22/2026, pg. 5), it is found unpersuasive.
It is acknowledged that the cited prior art does not expressly teach a sequence comprising D-enantiomers of certain amino acids; however the sequence taught by Krishna (i.e., IALILEPXCCQERAA, wherein X is Sar, represented by SEQ ID NO: 11 ) is 98.6% identical to instant SEQ ID NO: 6, as evidenced by the GenCore Sequence Alignment. Since the scope of claims 1, 5, and 13 encompass a sequence at least about 95% identical to an amino acid sequence selected from the group consisting of SEQ ID NOs: 6-13. Thus Krishna’s sequence reads on the instantly claimed invention, because the phrase at least about 95% encompasses sequences that are 95% identical or more than 95% identical to the elected species (i.e., SEQ ID NO: 6; IALILEPXCCQERAA, wherein X is Sar, and Leu at position 3 is D-Leu). Thereby the Krishna’s disclosure anticipates instant claims 1, 5 and 13.
In response to Applicants’ arguments pertaining to the NSDP rejections (see Remarks, filed 05/22/2026, pg. 6), have been fully considered, but are not persuasive.
It is noted that the features upon which applicant relies the many different properties (i.e., inhibition of CTLA-4 interaction with its cognate receptors and inhibition of CTLA-4 mediated signaling in a cell-based bioassay, inhibition of human T-cell exhaustion, inhibition of complement activation in human kidney carcinoma cell lines, and increase survival and quality of life in a mouse TC-1 tumor cell model) (see Remarks, filed 05/22/2026, pg. 6) are not recited in the rejected claims. Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Therefore, the scope of claim 1 and dependent claims do not correlate the functions which Applicants rely on.
Even if the scope of the instant claim encompassed the functions attributed to the sequences comprising D-enantiomeric forms of the amino acids or stapled modifications; and assuming arguendo that the cited art does not expressly teach those functions. Since the prior art teaches that a D-scan is a powerful strategy for studying how the stereochemistry of amino acids affects the structure and function of proteins; it would naturally follow that Krishna’s SEQ ID NO: 11, when modified at position 3 by substituting Leu for D-Leu would necessarily exhibit the same functions.
As such, the reasons an ordinary skilled artisan would modify the teachings of Krishna and substitute Leu at position 3 with D-Leu, does not preclude a finding of obviousness. In other words, it is not necessary for the prior art (i.e., copending applications and the issued patents) to teach the different properties and functions of the sequences that read on the instant invention.
Accordingly, the NSDP Obviousness rejections are appropriate and have been maintained.
Conclusion
No claims are allowed.
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/CLAUDIA ESPINOSA/Patent Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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