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 .
Detailed Action
Claims 1-27 are pending in the instant application.
Election/Restrictions
Applicant elected without traverse Group 1 (claims 1-11, 13 and 24-27) drawn to an analogue and without traverse compound 30 in the response filed April 10, 2026.
The restriction is deemed proper and is made FINAL in this office action. Claims 19-21 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected
invention/species, there being no allowable generic or linking claim.
Claims 1-11, 13, 24-27 are examined on the merits of this office action.
Sequence Compliance
This application fails to comply with the requirements of 37 C.F.R 1.821-1.825 for the reasons set forth on the attached Notice to Comply With Requirements For Patent Applications Containing Nucleotide Sequence And/or Amino Acid Sequence Disclosures. Applicant must comply with the requirements of the sequence rules (37 CFR 1.821-1.825) before the application can be examined under 35 U.S.C 131 and 132. Each sequence disclosed must appear separately in the “Sequence Listing.” Each sequence set forth in the “Sequence Listing” must be assigned a separate sequence identifier. Applicant failed provide sequence identifiers for all sequences listed in claims. For example, please see claims 5 and 6.
Claim Objection
Claims 5-6 are objected to for the following reason: Claims5-6 recite amino acid sequences. The peptide sequences are missing the sequence identifier. The proper way to claim a peptide sequence is for example, EGSA (SEQ ID NO: 2), for example (see 37 CFR 1.821(d)). This error should be corrected.
Claim 3 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 5 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 6 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 7 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 8 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 9 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 10 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 11 is objected to for the following informality: the limitation of “A compstatin…” should be replaced with -The
Claim 13 is objected to for the following informality: the limitation of “comprising a compstatin…” should be replaced with -comprising [[a]]the compstatin-
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 1-11, 13, 24-27 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 1-2, 4 claim “R2 is absent or is a sequence of 1 to 6 amino acid residues selected from…” The phrase is internally unclear because “comprising” is open-ended, while “1 to 6 amino acid residues” appears to impose a closed numerical limit. Thus, it is unclear whether R2 is limited to a sequence having no more than 6 amino acid residues or whether R2 may include more than 6 amino acid residues, or whether R2 may include additional residues or other moieties beyond the recited 1 to 6 residues. Accordingly, the metes and bounds of R2 cannot be determined with reasonable certainty. Claims 3, 5-6, 10-11 and 13 depend on claim 1 and do not further clarify this point of confusion and thus are also rejected. Claims 24-27 ultimately depend on claim 1 (via claim 6) and do not further clarify this point of confusion and thus are also rejected.
Claims 7-8 recites “wherein the peptide backbone is selected from”, followed by structures containing not only peptide sequence information, but also side chain modifications, bridge annotations, PEG substituents, lipid moieties, and terminal modifications. Claim 1, from which claim 7 depends on, does not recite or define a “peptide backbone” and thus lacks antecedent basis. Accordingly, it is unclear what portion of the claimed compound constitutes the “peptide backbone”, and therefore unclear what subject matter claim 7 is intended to limit. The scope of claims 7 and 8 cannot be determined with reasonable certainty because a person of ordinary skill in the art would not understand whether the listed entries represent complete compounds, peptide sequences, or only backbone structures (see MPEP 2173.05(e)). Claim 9 is also rejected due to its dependence on claim 8 and not further clarifying these points of confusion.
Claim 25 recites that “Z² is a sequence of 1 to 6 residues of compounds selected from” a list including amino acids, linker moieties, PEG groups, and non-amino-acid compounds. The scope of the term “residues” is unclear because the listed compounds include both amino acid residues and non-peptidic chemical moieties, such as 8-amino-3,6-dioxaoctanoic acid (Peg3), 11-amino-3,6,9-trioxaundecanoic acid (Peg4), and (piperazine-1-yl)-carboxylic acid. Accordingly, it is unclear whether “residues” refers exclusively to amino acid residues, chemical linker units parts of the listed compounds, or any combination thereof. Therefore, the metes and bounds of the claimed sequence cannot be determined with reasonable certainty. Claims 26-27 is also rejected due to its dependence on claim 25 and not further clarifying this point of confusion.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1, 3, 5, 10-11, 13 is/are rejected under 35 U.S.C. 103 as being unpatentable over Grossi (WO2019118938 A1, cited in IDS) in view of Cramer (Chem. Sci., 2016, 7, 7007, cited in IDS).
Grossi teaches a compstatin analogue comprising the sequence Ac-ICVWQDWGAHRCT-CONH2 wherein Y1 is acetyl, R1 is absent, X1 is Ile, X3 is Val, X4 is Trp, X6 is Asp, X8 is Gly, X9 is Ala, X11 is Arg, X13 is Thr and Y2 is NH2 and R2 is absent. Gross teaches wherein there is a disulfide bond between cysteine residues (see paragraph 0096). Grossi teaches the disulfide can be replaced with other linkages such as a thioether bond (see paragraph 0096). Regarding claim 5, Grossi teaches wherein R1 is dY meeting the limitations of instant claim 5 (see paragraph 0125, “B1”). Regarding claims 11 and 13, Grossi teaches inclusion in a pharmaceutical formulation with a carrier (see claims 111, 113).
Grossi is silent to wherein the bridge is a C1-3 alkylene bridge between the Sulphur atoms of the cysteine residues.
However, Cramer teaches of converting disulfide bridges to stable methylene thioacetals (see abstract). Cramer teaches of “a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained”(see abstract).
It would have been obvious before the effective filing date of the claimed invention to one of ordinary skill in the art to replace the disulfide linkage of Grossi with a C1-C3 alkylene bride between the sulfur atoms of the cysteine residues, as taught by Cramer, in order to improve peptide stability while retaining biological activity. Grossi expressly teaches compstatin analogues containing cysteine linked cyclic structures and further teaches that the disulfide linkage may be replaced with alternative linkages such as thioether bonds. Cramer teaches that disulfide bridges in peptides may be converted to stable methylene thioacetals under mild, biocompatible conditions, resulting in enhanced serum, pH and temperature stability while maintaining biological function. One of ordinary skill in the art would have been motivated to apply the bridge modification taught by Cramer to the cyclic compstatin analogues with retained activity. Further, because Cramer teaches that methodology is broadly applicable to peptides and preserves biological activity, there would have been a reasonable expectation of success in modifying the Grossi peptides to includes the claimed C1-3 alkylene bridge. Regarding claim 10, the combined references teach use of a methylene bridge thus meeting the limitations of instant claim 10.
Claims 1-11, 13, 24-27 is/are rejected under 35 U.S.C. 103 as being unpatentable over Shelton (WO2019166411 A1, cited in IDS) in view of Cramer (Chem. Sci., 2016, 7, 7007, cited in IDS, cited in IDS).
Regarding claims 1-4, Shelton teaches a compstatin analogue comprising the sequence SEFC(1 )l[1-Me-Trp]QDWGEHRC(1)TGAES-[K*] wherein Y1 is hydrogen, R1 is SE, X1 is Phe, X3 is Ile, X4 is 1-Me-Trp, X6 is Asp, X8 is Gly, X9 is Glu, X11 is Arg, X13 is Thr, R2 is GAES and Y2 lipophilic group (claim 23, compound 135). Regarding claim 5, Shelton teaches wherein R1 is SE Regarding claim 6, Shelton teaches wherein R2 comprises GAES (see claim 23).
Shelton teaches wherein there is a disulfide bond between cysteine residues (see page 10, lines 30-31).. Regarding claims 11 and 13, Shelton teaches inclusion in a pharmaceutical formulation with a carrier (see page 21, lines 20-21).
Shelton is silent to wherein the bridge is a C1-3 alkylene bridge between the Sulphur atoms of the cysteine residues as the linkage.
However, Cramer teaches of converting disulfide bridges to stable methylene thioacetals (see abstract). Cramer teaches of “a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained”(see abstract).
It would have been obvious before the effective filing date of the claimed invention to one of ordinary skill in the art to replace the disulfide linkage of Shelton with a C1-C3 alkylene bride between the sulfur atoms of the cysteine residues, as taught by Cramer, in order to improve peptide stability while retaining biological activity. Cramer teaches that disulfide bridges in peptides may be converted to stable methylene thioacetals under mild, biocompatible conditions, resulting in enhanced serum, pH and temperature stability while maintaining biological function. One of ordinary skill in the art would have been motivated to apply the bridge modification taught by Cramer to the cyclic compstatin analogues with retained activity. Further, because Cramer teaches that methodology is broadly applicable to peptides and preserves biological activity, there would have been a reasonable expectation of success in modifying the Shelton peptides to includes the claimed C1-3 alkylene bridge.
Regarding claims 7-9, the combined references of Shelton in view of Cramer teach wherein the cysteines are linked via a methylene bridge. Thus, the compounds taught by Shelton, including compound 135/compound 67 of Shelton meet the limitations of the claims.
Regarding claim 10, the combined references teach use of a methylene bridge thus meeting the limitations of instant claim 10.
Regarding claim 24, Shelton teaches wherein K* is a lysine covalent linked to a lipophilic group (see claim 12 for example).
Regarding claim 25, Shelton teaches wherein the lipophilic group is Z1 or Z1-Z2, wherein Z1 is A-C12-22alkylene-CO (see page 104, claim 27).
Regarding claim 26, Shelton teaches wherein Z1 is H(CH2)11-CO (see claim 28).
Regarding claim 27, Shelton teaches wherein Z1 is 17-carboxyheptadecanoyl, i.e. HOOC-(CH2)15-(CO)- (see claim 28).
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.
Claims 1-11, 13, 24-27 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. US12600749 B2 in view of Cramer (see above reference). Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims a compstatin analogue of formula I Y1-R1-X1-C-X3-X4-Q-X6-W-X8-X9-H-X11-C-X13-R2-Y2 (I) with variables defined in instant claim 1 and additionally a C1-C3 alkylene bridge. Instant claim 5 claims wherein R1 is dY (see claim 5); E[PEG3][PEG3]lys (Claim 6); methylene alkylene bridge (claim 10); pharmaceutical formulations (Claim 11); wherein the Lys is attached to a lipophilic group (claim 24); Z1 is the lipophilic group of C12-22 alkylene CO (claims 25-26); or 19-carboxy-noadecanyol[yglu]G[yglu] (claim 27). The instant application claims compounds 1-31 (instant claims 7-9) which a specific sequence of formula I.
US Patent No. ‘749 claims “A method of inhibiting complement activation for treating a subject in need thereof, the method comprising administering to the subject a compstatin analogue of Formula I:
(SEQ ID NO: 2) Y1-R1-X1-C-I-X4-Q-X6-W-X8-E-H-X11-C-X13-R2-Y2 (Formula I)” which over laps with the instant claims. US Patent No. ‘749 further claims a disulfide linkage between C1 and C2; and compounds that overlap with instant claims 7-9 (see claim 11 , compound 135 for example). US Patent No. ‘749 further claims wherein the compstatin analogue comprises a lipophilic group φ, and wherein the lipophilic group φ is Z1 or Z1-Z2 (claims 12-15) which are identical to the instant claims; and pharmaceutical formulations thereof (see claims 17-18).
US Patent No. ‘749 is silent to an alkylene (or methylene bond) between cysteines as found in the instant claims.
However, Cramer teaches of converting disulfide bridges to stable methylene thioacetals (see abstract). Cramer teaches of “a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained”(see abstract).
It would have been obvious before the effective filing date of the claimed invention to one of ordinary skill in the art to replace the disulfide linkage of US Patent No. ‘749 with a C1-C3 alkylene bride between the sulfur atoms of the cysteine residues, as taught by Cramer, in order to improve peptide stability while retaining biological activity. Cramer teaches that disulfide bridges in peptides may be converted to stable methylene thioacetals under mild, biocompatible conditions, resulting in enhanced serum, pH and temperature stability while maintaining biological function. One of ordinary skill in the art would have been motivated to apply the bridge modification taught by Cramer to the cyclic compstatin analogues with retained activity. Further, because Cramer teaches that methodology is broadly applicable to peptides and preserves biological activity, there would have been a reasonable expectation of success in modifying the US Patent No. ‘749 peptides to includes the claimed C1-3 alkylene bridge.
Claims 1-11, 13, 24-27 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-35 of U.S. Patent No. US11965039 B2 in view of Cramer (see above reference). Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims a compstatin analogue of formula I Y1-R1-X1-C-X3-X4-Q-X6-W-X8-X9-H-X11-C-X13-R2-Y2 (I) with variables defined in instant claim 1 and additionally a C1-C3 alkylene bridge. Instant claim 5 claims wherein R1 is dY (see claim 5); E[PEG3][PEG3]lys (Claim 6); methylene alkylene bridge (claim 10); pharmaceutical formulations (Claim 11); wherein the Lys is attached to a lipophilic group (claim 24); Z1 is the lipophilic group of C12-22 alkylene CO (claims 25-26); or 19-carboxy-noadecanyol[yglu]G[yglu] (claim 27). The instant application claims compounds 1-31 (instant claims 7-9) which a specific sequence of formula I.
US Patent No. ‘039 claims “ A compstatin analogue represented by the formula:Y1-R1-X1-C-I-X4-Q-X6-W-X8-E-H-X11-C-X13-R2-Y2 (Formula I) (SEQ ID NO: 327)” which over laps with the instant claims. US Patent No. ‘039 further claims a disulfide linkage between C1 and C2 (Claim 1); and compounds that overlap with instant claims 7-9 (see claim 22 , compound 135 for example). US Patent No. ‘039 further claims wherein the compstatin analogue comprises a lipophilic group φ, and wherein the lipophilic group φ is Z1 or Z1-Z2 (claims 25-27) which are identical to the instant claims; pharmaceutical formulations (claims 30-32).
US Patent No. ‘039 is silent to an alkylene (or methylene bond) between cysteines as found in the instant claims.
However, Cramer teaches of converting disulfide bridges to stable methylene thioacetals (see abstract). Cramer teaches of “a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained”(see abstract).
It would have been obvious before the effective filing date of the claimed invention to one of ordinary skill in the art to replace the disulfide linkage of US Patent No. ‘039 with a C1-C3 alkylene bride between the sulfur atoms of the cysteine residues, as taught by Cramer, in order to improve peptide stability while retaining biological activity. Cramer teaches that disulfide bridges in peptides may be converted to stable methylene thioacetals under mild, biocompatible conditions, resulting in enhanced serum, pH and temperature stability while maintaining biological function. One of ordinary skill in the art would have been motivated to apply the bridge modification taught by Cramer to the cyclic compstatin analogues with retained activity. Further, because Cramer teaches that methodology is broadly applicable to peptides and preserves biological activity, there would have been a reasonable expectation of success in modifying the US Patent No. ‘039 peptides to includes the claimed C1-3 alkylene bridge.
Claims 1-11, 13, 24-27 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5-6, 8-9, 16-18, 21-24, 30, 33, 36-40, 43-45, 56-59 of copending Application No. 17/637392 (reference application) in view of Cramer (see above reference). Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims a compstatin analogue of formula I Y1-R1-X1-C-X3-X4-Q-X6-W-X8-X9-H-X11-C-X13-R2-Y2 (I) with variables defined in instant claim 1 and additionally a C1-C3 alkylene bridge. Instant claim 5 claims wherein R1 is dY (see claim 5); E[PEG3][PEG3]lys (Claim 6); methylene alkylene bridge (claim 10); pharmaceutical formulations (Claim 11); wherein the Lys is attached to a lipophilic group (claim 24); Z1 is the lipophilic group of C12-22 alkylene CO (claims 25-26); or 19-carboxy-noadecanyol[yglu]G[yglu] (claim 27). The instant application claims compounds 1-31 (instant claims 7-9) which a specific sequence of formula I.
The copending application claims compstatin analogue of formula I which overlaps with instant claim 1; lipophilic groups (claim 5); R1 has a sequence dY or E as found in instant claim 5; EA[PEG3][PEG43]K (claim 21); wherein the Lys is attached to a lipophilic group; Z1 is the lipophilic group of C12-22 alkylene CO; or 19-carboxy-noadecanyol[yglu]G[yglu] (Claim 37). The copending application claims compounds that overlap with instant claims 7-9 (see claim 30 , compound 135 for example).
Co pending application claims a thioether bond between X2 and X12 instead of an alkylene (or methylene bond) as found in the instant claims.
However, Cramer teaches of converting disulfide bridges to stable methylene thioacetals (see abstract). Cramer teaches of “a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained”(see abstract).
It would have been obvious before the effective filing date of the claimed invention to one of ordinary skill in the art to replace the disulfide linkage of Copending AN 17/637392 with a C1-C3 alkylene bride between the sulfur atoms of the cysteine residues, as taught by Cramer, in order to improve peptide stability while retaining biological activity. Cramer teaches that disulfide bridges in peptides may be converted to stable methylene thioacetals under mild, biocompatible conditions, resulting in enhanced serum, pH and temperature stability while maintaining biological function. One of ordinary skill in the art would have been motivated to apply the bridge modification taught by Cramer to the cyclic compstatin analogues with retained activity. Further, because Cramer teaches that methodology is broadly applicable to peptides and preserves biological activity, there would have been a reasonable expectation of success in modifying the copending AN 17/637392 peptides to includes the claimed C1-3 alkylene bridge.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERINNE R DABKOWSKI whose telephone number is (571)272-1829. The examiner can normally be reached Monday-Friday 7:30-5:30 Est.
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/ERINNE R DABKOWSKI/ Examiner, Art Unit 1654
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