DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant's election without traverse of Group I (Invention I) in the reply filed on 07/23/2026 is acknowledged. Claims 15-17 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention. The requirement is still deemed proper and is therefore made FINAL.
Claims 1-14, 18, 19 are under consideration in this Office Action.
Title
The title of the invention is not descriptive. A new title is required that is clearly indicative of the invention to which the claims are directed.
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 of this title, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1-14, 18, 19 are rejected under 35 U.S.C. 103 as being unpatentable over Accession I61596 (24-May-1996; PTO 892) in view of Putranto et al. ( (2013) Inhibition of RAGE signalling through the intracellular delivery of inhibitor peptides by PEI cationization. Int J Mol Med., 32, 938-944; IDS filed 05/07/2025), US20090220484A1 (2009-09-03; PTO 892), Bornscheuer et al. (Curr Protoc Protein Sci. 2011 Nov;Chapter 26:Unit26.7; PTO 892).
Accession I61596 teaches human glycoprotein receptor RAGE comprising the polypeptide fragment having the amino acid sequence of SEQ ID NO: 14 of the instant application (see attached alignment). The teachings of the reference differ from the claims in that the reference does not teach the claimed peptide that inhibits RAGE ligand-independent signalling.
Putranto et al. teach the following peptides derived from the cytoplasmic domain of RAGE (aa 387-395): "RAGE(E)-I" which has the sequence WENQEEEEERAELNQEEEPE and
contains mutation S391 E; and "RAGE(A)-I" which has the sequence WENQAEAEERAELNQAEAPE and contains mutation S391A. Putranto et al. teach that the peptide RAGE(E)-I inhibits ligand-dependent RAGE signalling by inhibiting
binding of TIRAP to RAGE while the peptide RAGE(A)-I does not. The peptides are biotinylated and complexed to PEl-avidin for intracellular delivery. The peptide RAGE(E)-I provides a powerful tool for therapeutics to block RAGE mediated multiple signaling. The peptide RAGE(E)-I comprises SEQ ID NO:6 of the present application. See entire publication and abstract especially Figure 1, Materials and methods section, Results section, and pages 939-941.
US20090220484A1 teaches a polypeptide consisting essentially of all or a portion of the cytoplasmic domain of RAGE, and further a polypeptide consisting essentially of a portion of Diaphanous that binds to the cytoplasmic domain of RAGE (see entire publication and claims especially paragraphs [0009]- [0019]). US20090220484A1 teaches the following in the claims:
1. An isolated polypeptide consisting essentially of all or a portion of the cytoplasmic domain of a RAGE protein.
2. The polypeptide of claim 1, wherein the RAGE protein is human RAGE.
4. A pharmaceutical composition comprising the polypeptide of claim 1 and a pharmaceutically acceptable carrier.
5. A polypeptide consisting essentially of all or a portion of the FH1 domain of a Diaphanous protein.
7. The polypeptide of claim 5, wherein the Diaphanous protein is human Diaphanous.
8. (canceled)
9. A pharmaceutical composition comprising the polypeptide of claim 5 and a pharmaceutically acceptable carrier.
Bornscheuer et al. teach protein engineering strategies to improve or change the properties of proteins, teach concepts for protein engineering using rational design including substitution and/or deletion of amino acids, directed evolution, and combinations of them where different strategies are presented for identifying the best mutagenesis method, how to identify desired variants by screening or selection, and examples for successful applications are shown which enable researchers to choose the most promising tools to solve their protein engineering challenges (see entire publication especially pages 26.7.1- 26.7.10 and Tables 26.7.1, 26.7.2, and 26.7.3).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the teach protein engineering strategies of Bornscheuer et al. on the polypeptide fragment of Accession I61596 having the amino acid sequence of SEQ ID NO: 14 of the instant application to make the peptide having the amino acid modifications recited in all of the claims, isolating modified polypeptide fragment that inhibits RAGE ligand-independent signalling and making fusion protein comprising the polypeptide fragment as taught by Putranto et al., and formulating a pharmaceutical composition comprising the modified polypeptide fragment and one or more excipients as taught by US20090220484A1. One of ordinary skill in the art before the effective filing date of the claimed invention would have been motivated to do this in order to obtain isolated or purified peptide for therapeutics to block RAGE mediated signaling as taught by Putranto et al. One of ordinary skill in the art at the time the invention was made would have a reasonable expectation of success because modifying peptide fragments to inhibit and/or block RAGE mediated signaling are known in the art as shown by the above reference teachings. Hence, the claimed invention as a whole is prima facie obvious.
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 obviousness-type 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); and 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 a nonstatutory double patenting ground provided the conflicting application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement.
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
Claims 1-14, 18, 19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-26 of US Patent 12060408. Although the conflicting claims are not identical, they are not patentably distinct from each other for the following reasons.
The claims and/or specification of the patents teach the claimed isolated or purified peptide that inhibits RAGE ligand-independent signalling, the peptide: (i) comprising an amino acid sequence that is at least 90% identical to a fragment of residues 22 to 404 of wild-type RAGE as set forth in SEQ ID NO: 14, wherein the peptide comprises at least both residues 379 and 391, and wherein the residue at 379 is not Q or a conservative amino acid substitution thereof; (ii) consisting of an amino acid sequence that is greater than 90% identical to a fragment of residues 22 to 404 of wild-type RAGE as set forth in SEQ ID NO: 14, wherein the peptide comprises at least both residues 379 and 391, wherein the residue at 379 is not Q or a conservative amino acid substitution thereof, or wherein the residue at 391 is not S or a conservative amino acid substitution thereof; (iii) comprising an amino acid sequence that is at least 95% identical to a fragment of residues 22 to 404 of wild-type RAGE as set forth in SEQ ID NO: 14, wherein the peptide comprises at least both residues 379 and 391, wherein the residue at 379 is not Q or a conservative amino acid substitution thereof, or wherein the residue at 391 is not S or a conservative amino acid substitution thereof; (iv) comprising an amino acid sequence that is at least 90% identical to a fragment of residues 22 to 404 of wild-type RAGE as set forth in SEQ ID NO: 14, wherein the peptide comprises at least both residues 379 and 391, wherein the residue at 379 is Q or a conservative amino acid substitution thereof, and the residue 391 is not S or a conservative amino acid substitution thereof or E; or (v) comprising an amino acid sequence that is at least 90% identical to a fragment of residues 22 to 404 of wild-type RAGE as set forth in SEQ ID NO: 14, wherein the peptide comprises at least both residues 379 and 391 and wherein if residue 376 is present it is not W, wherein the residue at 379 is not Q or a conservative amino acid substitution thereof, or wherein the residue at 391 is not S or a conservative amino acid substitution thereof. Thus, the teachings anticipate the claimed invention.
Conclusion
No claims are allowed.
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/CHRISTIAN L FRONDA/Primary Examiner, Art Unit 1652
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