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 1-16 are pending in the instant application.
Election/Restrictions
Applicant elected with traverse Group 1 (claims 1-12) drawn to a peptide and with traverse SEQ ID NO:1 wherein X1 is A, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is N, X7 is L and X8 is L from List I and buffered salt solution from List II in the response filed January 20, 2026.
The restriction is deemed proper and is made FINAL in this office action. Claims 3, 7, 9, 13-16 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected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 1-2, 4-6, 8, 10-12 are examined on the merits of this office action.
Claim Objection
Claim 5 is objected to for the following informality: the limitation of “wherein the peptides” should be replaced with -wherein the peptide[[s]]-.
Claim 6 is objected to for the following informality: the limitation of “comprising a peptide” should be replaced with -comprising [[a]] the peptide-.
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 10-12 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.
Claim 10 claims “said peptide being in operable combination with a promoter”. However, a promoter is a nucleic acid regulatory element that functions when operably linked to a nucleic acid sequence, not a peptide. Thus, it is unclear how a peptide can be in “operable combination” with a promoter. Accordingly, the relationship recite is technically unclear, and one of ordinary skill in the art would not be able to determine the metes and bounds of the claimed invention with a reasonably certainty. A suggested amendment would be….”wherein the nucleic acid is operably linked to a promoter”. Claims 11-12 are also rejected due to their dependence on claim 10 and not clarifying this point of confusion.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 4, 6, 8 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Gozes (US6630124 B1).
Gozes discloses the peptide R1-Lys-Pro-Arg-Arg-Pro-Tyr-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-X1-Ala-X2-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH-R2 wherein X1 is nor leucine and X2 is valine, R1 is H and R2 is H thus meeting the limitations of instant claim 1 wherein instant X1 is any amino acid (thr) X2 is any amino acid (Asp), X3 is any amino acid (Tyr), X4 is any amino acid (Arg), X5 is any amino acid (norleucine); X6 is any amino acid (Lys); X7 is any amino acid (leu); X8 is any amino acid (Ser) and not comprising instant SEQ ID NO:1. Regarding claim 4, the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Regarding claim 6, Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Regarding claim 8, Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
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, 4-6, 8 is/are rejected under 35 U.S.C. 103 as being unpatentable over Gozes (US6630124 B1) in view of Chandrasekharan (Am J Physiol Gastrointest Liver Physiol 304: G949–G957, 2013) and Pankove (Journal for ImmunoTherapy of Cancer 2017, 5(Suppl 2):P153 ).
Gozes discloses the peptide R1-Lys-Pro-Arg-Arg-Pro-Tyr-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-X1-Ala-X2-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH-R2 wherein X1 is norleucine and X2 is valine, R1 is H and R2 is H thus meeting the limitations of instant claim 1 wherien instant X1 is any amino acid (thr) X2 is any amino acid (Asp), X3 is any amino acid (Tyr), X4 is any amino acid (Arg), X5 is any amino acid (norleucine); X6 is any amino acid (Lys); X7 is any amino acid (leu); X8 is any amino acid (Ser) and not comprising instant SEQ ID NO:1. Regarding claim 4, the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Regarding claim 6, Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Regarding claim 8, Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
Gozes is silent to linking the VIP peptides to nanoparticles.
Pankove teaches nanoparticle conjugates comprising a VIP antagonist (VIPhyb) targeted to tumor draining lymph nodes to enhance anti-tumor immune responses. Pankove demonstrates that nanoparticle delivery can improve targeting and immunomodulatory effects in a cancer context.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of Gozes to be delivered using a nanoparticle based delivery system as taught by Pankove and Chandrasekharan. In view of the teachings of Pankove and Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of Gozes into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Claims 1, 4, 6, 8, 10-12 is/are rejected under 35 U.S.C. 103 as being unpatentable over Gozes (US6630124 B1) in view of Gersbach (Engineered Bioactive molecules, Duke, 2011, chapter 5.510) and Thermo (Protein Expression Overview, 2016).
Gozes discloses the peptide R1-Lys-Pro-Arg-Arg-Pro-Tyr-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-X1-Ala-X2-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH-R2 wherein X1 is norleucine and X2 is valine, R1 is H and R2 is H thus meeting the limitations of instant claim 1 wherein instant X1 is any amino acid (thr) X2 is any amino acid (Asp), X3 is any amino acid (Tyr), X4 is any amino acid (Arg), X5 is any amino acid (norleucine); X6 is any amino acid (Lys); X7 is any amino acid (leu); X8 is any amino acid (Ser) and not comprising instant SEQ ID NO:1. Regarding claim 4, the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Regarding claim 6, Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Regarding claim 8, Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
Gozes is silent to DNA encoding said peptide (VPP antagonist) above, a recombinant vector comprising the nucleic acid sequence and a cell comprising said vector (basically making the protein via recombinant DNA technology). Gozes does teach peptide synthesis (see column 8, lines 38-50).
However, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide disclosed by Gozes represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143?).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
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, 4-6, 8, 10-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11471506 in view of Gozes, Chandrasekharan, Pankove, Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprisingKPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
US Patent No. ‘506 claims “A method of enhancing the immune response to a cancer or treating a cancer in a subject in need thereof comprising administering an antagonist of vasoactive intestinal peptide signalling in combination with an antibody to immune check-point molecule to the subject, wherein the cancer is leukemia, melanoma, pancreatic cancer, Hodgkin lymphoma, bladder cancer, kidney cancer, colon cancer, lung cancer, or breast cancer, and wherein the antibody to immune check-point molecule is an anti-PD-1 antibody or an anti-PD-L1 antibody” (claim 1). US Patent No. ‘506 further claims wherein the VIP antagonist is N-terminal Stearyl, Norleucine 17 VIPhyb, i.e., (SEQ ID NO: 9) KPRRPYTDNYTRLRKQXAVKKYLNSILN, wherein X is nor leucine (claim 9).
US Patent No. ‘506 is silent to including a pharmaceutical excipient; buffered aqueous salt solution; nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for treating cancer. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill int eh art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Regarding linking to nanoparticles, Pankove teaches nanoparticle conjugates comprising a VIP antagonist (VIPhyb) targeted to tumor draining lymph nodes to enhance anti-tumor immune responses. Pankove demonstrates that nanoparticle delivery can improve targeting and immunomodulatory effects in a cancer context.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of US Patent No. ‘506 to be delivered using a nanoparticle based delivery system as taught by Pankove and Chandrasekharan. In view of the teachings of Pankove and Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of US Patent No. ‘506 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143?).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
Claims 1, 4-6, 8, 10-11, 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. Patent No. 12098180 in view of Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprising KPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
US Patent No. ‘180 claims “A peptide comprising the amino acid sequence KPRRPYTDNYTRLRKQMAVKKYLNLILN (SEQ ID NO: 10)” (claim 1). US Patent No. ‘180 further claims the peptide conjugated to a nanoparticle (claim 2); a pharmaceutically acceptable excipient (Claim 3); sterilized pH buffered aqueous salt solution (claim 5).
US Patent No. ‘180 is silent to nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143?).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
Claims 1, 4-6, 8, 10-11, 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11464855 in view of Gozes, Chandrasekharan, Pankove, Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprisingKPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
US Patent No. ‘855 claims “A method of treating a human subject diagnosed with leukemia comprising administering bone marrow cells in combination with an effective amount of a composition consisting of a vasoactive intestinal peptide (VIP) antagonist, wherein the VIP antagonist is a peptide antagonist to the subject in need thereof, wherein treatment is to treat leukemia; wherein the VIP antagonist is a peptide having a C-terminal amide and is optionally modified with hydrocarbon or polyethylene glycol groups and wherein the peptide has the sequence of SEQ ID NO: 9 wherein X is M; and wherein the bone marrow cells comprise CD8+T cells” (claim 1).
US Patent No. ‘855 further claims wherein the VIP antagonist is N-terminal Stearyl, Norleucine 17 VIPhyb, i.e., (SEQ ID NO: 9) KPRRPYTDNYTRLRKQXAVKKYLNSILN, wherein X is nor leucine (claim 9) which falls within the scope of instant claims 1.
US Patent No. ‘855 is silent to including a pharmaceutical excipient; buffered aqueous salt solution; nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for treating cancer. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Regarding linking to nanoparticles, Pankove teaches nanoparticle conjugates comprising a VIP antagonist (VIPhyb) targeted to tumor draining lymph nodes to enhance anti-tumor immune responses. Pankove demonstrates that nanoparticle delivery can improve targeting and immunomodulatory effects in a cancer context.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of US Patent No. ‘855 to be delivered using a nanoparticle based delivery system as taught by Pankove and Chandrasekharan. In view of the teachings of Pankove and Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of US Patent No. ‘855 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
Claims 1, 4-6, 8, 10-11, 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 9669092 in view of Gozes, Chandrasekharan, Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprisingKPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
US Patent No. ‘092 claims “A method of treating an active cytomegalovirus infection comprising administering an effective amount of a vasoactive intestinal peptide antagonist to a subject diagnosed with and exhibiting signs or symptoms of an active cytomegalovirus infection, wherein the vasoactive intestinal peptide antagonist comprises a peptide having a C-terminal amide and is optionally modified with hydrocarbon or polyethylene glycol groups and wherein the peptide has SEQ ID NO: 9, wherein X is M” (claim 1). SEQ ID NO:9 of US Patent No. ‘092 falls within the scope of instant claim 1 (the VIP antagonist is N-terminal Stearyl, Norleucine 17 VIPhyb, i.e., (SEQ ID NO: 9) wherein X is M).
US Patent No. ‘092 is silent to including a pharmaceutical excipient; buffered aqueous salt solution; nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for therapeutic treatment. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of US Patent No. ‘092 to be delivered using a nanoparticle based delivery system as taught by Chandrasekharan. In view of the teachings of Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of US Patent No. ‘092 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
Claims 1, 4-6, 8, 10-11, 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-23 of co-pending AN18/047135 view of Gozes, Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprisingKPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
Co-pending Application 18/047135 claims “A method of treating a cancer in a subject comprising obtaining a T cell; exposing the T cell in vitro or ex vivo to a vasoactive intestinal polypeptide (VIP) antagonist and an immune check-point inhibitor thereby expanding the T cell; and administering an effective amount of the expanded T cell to the subject” (claim 1).
Co-pending Application 18/047135 further claims wherein the VIP antagonist is N-terminal Stearyl, Norleucine 17 VIPhyb, i.e., (SEQ ID NO: 9) KPRRPYTDNYTRLRKQXAVKKYLNSILN, wherein X is nor leucine (claim 13) which falls within the scope of instant claims 1. Co-pending Application 18/047135 further claims conjugation to a nanoparticle (claim 14).
Co-pending Application 18/047135 is silent to including a pharmaceutical excipient; buffered aqueous salt solution; nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence.
However, Gozes teaches VIP antagonist peptides for therapeutic purposes. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1, 4-6, 8, 10-11, 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 17-23, 25, 28-35 of co-pending AN18/045,317 view of Gozes, Chandrasekharan, Gersbach and Thermo (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprising KPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
Co-pending Application 18/045317 claims “A method of expanding a T cell in vitro by exposing T cell to a vasoactive intestinal peptide (VIP) antagonist; wherein the VIP antagonist is a peptide having a C-terminal amide” (claim 1). Co-pending Application 18/045317 claims “wherein the VIP antagonist is modified with hydrocarbon or polyethylene glycol groups and wherein the peptide consists of SEQ ID NO: 9, wherein X is M” (claim 20).
Co-pending Application 18/045317 further claims wherein the VIP antagonist is N-terminal Stearyl, Norleucine 17 VIPhyb, i.e., (SEQ ID NO: 9) KPRRPYTDNYTRLRKQXAVKKYLNSILN, wherein X is nor leucine (claim 13) which falls within the scope of instant claims 20.
Co-pending Application 18/045317 is silent to including a pharmaceutical excipient; buffered aqueous salt solution; nucleic acid sequence encoding the peptide, vectors and cells comprising said nucleic acid sequence and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for therapeutic treatment. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of Co-pending Application 18/045317 to be delivered using a nanoparticle based delivery system as taught by Chandrasekharan. In view of the teachings of Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of Co-pending Application 18/045317 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Regarding DNA and expression thereof, Gersbach teaches there are two general strategies for engineering bioactive peptides and proteins, recombinant DNA expression and synthetic polymerization. Gersbach teaches “The recombinant DNA approach uses genetically encoded sequences to generate the desired polypeptide. The engineer must first design a recombinant DNA segment that precisely encodes for the therapeutic protein of interest. This segment is then cloned into a suitable DNA plasmid to create a recombinant DNA molecule that can be delivered to cells with the appropriate machinery for express sing the desired protein. This plasmid is transformed into the host cells, which are then grown in culture for a prescribed length of time to allow for protein expression. The protein of interest is then purified from the cells or culture media” (see section 5.510.2.25). Gersbach further teaches short DNA sequences can be directly synthesized using standard solid-phase synthesis. For long proteins with repeating units, including many structural ECM proteins such as elastin, these shorter DNA sequences can be assembled into larger proteins that encode for repetitive structures of the desired molecular weight (see section 5.510.2.25). Gersbach teaches “Recombinant protein expression has many advantages over chemical synthesis. It provides well-defined sequences, stereo chemistry, and molecular weight based on the engineered genetic template” (see section 5.510.2.25, right column, second paragraph).
Thermo teaches that the gene of interest is included in a expression cassette (a vector) with a promoter (see Figure 1.3) for translation to occur.
It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique to the peptide disclosed represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
It would have been obvious to one of ordinary skill in the art to try recombinant DNA expression to produce the claimed peptide/protein, as recombinant expression was one of a finite number of well-known and routine methods available for protein production at the time of the invention. A skilled artisan would have had a reason to pursue recombinant expression as a predictable and commonly used approach for generating proteins with defined sequences. The selection of using recombinant expression to make the peptide would have been obvious to try, and a person of ordinary skill in the art would have had a reasonable expectation of success in producing the peptide using such techniques (see MPEP 2143 I(E)).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-2, 4-6, 8, 10-11, 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of co-pending AN18/715543 view of Gozes, Chandrasekharan (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprising KPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
Co-pending Application 18/715543 claims “A method of expanding a T cell in vitro by exposing T cell to a vasoactive intestinal peptide (VIP) antagonist; wherein the VIP antagonist is a peptide having a C-terminal amide” (claim 1). Co-pending Application 18/715543 claims wherein the VIP antagonist is SEQ ID NO:11 (claim 13) and nucleic acids sequences and vectors thereof (Claims 11, 14) which fall within the scope of instant claims 1-2 and 10;
Co-pending Application 18/715543 is silent to including a pharmaceutical excipient; buffered aqueous salt solution and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for therapeutic treatment. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of Co-pending Application 18/715543 to be delivered using a nanoparticle based delivery system as taught by Chandrasekharan. In view of the teachings of Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of Co-pending Application 18/045317 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Furthermore, It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 1-2, 4-6, 8, 10-11, 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 6, 9, 13-14, 31-32, 40, 42, 49-51, 58-60, 67-68, 72-74 of co-pending AN18/562111 view of Gozes, Chandrasekharan (all references cited above).
Although the claims at issue are not identical, they are not patentably distinct from each other because:
The instant application claims “peptide comprising KPRRPYXX2NX3TX4LRKQX5AVX6KY X7 N X8 I L N (SEQ ID NO: 11), wherein X is A or any amino acid;X2 is V or any amino acid; X3 is C or any amino acid; X4 is S or any amino acid; X5 is I or any amino acid; X6 is N or any amino acid; X7 is M or any amino acid; X8 is I or any amino acid; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1) or the combination wherein X is T, X2 is D, X3 is Y, X4 is R, X5 is M, X6 is K, X7 is L, and X8 is S” (claim 1). The instant application further claims SEQ ID NO:11 as defined in instant claim 2; wherein a carboxyl group is substituted (claim 4); excipient (claim 6); sterilized pH buffered aqueous salt solution (claim 8); nucleic acid sequence encoding SEQ ID NO:11 as defined in instant claim 10; a recombinant vector comprising said nucleic acid sequence (claim 11); and a cell comprising the vector (claim 12).
Co-pending Application 18/562111 claims VIP antagonists that fall with the scope of instant claims 1-2 (see claim 3) and nucleic acid sequences thereof (see claim 9). Co-pending Application 18/562111 further claims including a carrier (Claim 6); methods of treatment (claims 40, 42, 49).
Co-pending Application 18/562111 is silent to including a buffered aqueous salt solution and linked to a nanoparticle.
However, Gozes teaches VIP antagonist peptides for therapeutic treatment. Gozes teaches that the carboxyl group of the last amino acid is substituted an NH2 (see claim 1). Gozes teaches pharmaceutical formulations comprising an acceptable carrier/excipient (see claim 1). Gozes teaches aqueous carriers may be used for example buffered water and saline solutions and that they can be sterilized (see column 16, lines 36-60).
It would have been obvious to one of ordinary skill in the art at the time of the invention to include a pharmaceutically acceptable carrier and to formulate the composition in a sterile buffered solution ,as such carriers and sterilized aqueous buffers (e.g. saline) are well known and routinely used in the art for the formulation and administration of peptide based therapeutics. Accordingly, these features represent routine formulation choices that would have been obvious.
Chandrasekharan teaches that neuropeptides, including VIP, have therapeutic potential but face significant challenges such as instability, limited bioavailability and multiple cellular targets. Chandrasekharan further teaches that nanoparticle based delivery systems are a desirable approach to targeting and delivery of neuropeptides (see page G954, “VIP vectors” and “Challenges in Therapy”).
It would have been obvious before the effective filing date of the claimed invention to modify the VIP peptide of Co-pending Application 18/715543 to be delivered using a nanoparticle based delivery system as taught by Chandrasekharan. In view of the teachings of Chandrasekharan, one of ordinary skill in the art would have been motivated to incorporate the VIP peptide of Co-pending Application 18/045317 into a nanoparticle delivery system in order to improve targeting and therapeutic effectiveness. Further, because nanoparticle delivery systems were known in the art for delivery peptide based therapeutics, there would have been a reasonable expectation of success in achieving an improved therapeutic outcome.
Furthermore, It would have been obvious before the effective filing date of the claim invention to employ recombinant DNA expression to produce the claimed peptide as recombinant expression systems were well known and routinely used for generating proteins with defined sequences in a controlled and scalable manner. Applying this known technique represents no more than the predictable use of prior art elements according to their established functions, yielding predictable results (see MPEP 2143).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claims are allowed.
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/ERINNE R DABKOWSKI/Examiner, Art Unit 1654
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