DETAILED ACTION Notice of Pre-AIA or AIA Status The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Priority The present Application, filed September 13, 2022 , is a Continuation-In-Part of U.S. Patent Application No. 16/765,962 (now U.S. Patent No. 11,471,502), filed May 21, 2020, which wa s a national stage entry under 35 U.S.C. § 371 of International Patent Application No. PCT/ GB2018 /05 3384 , filed November 23, 2018, which claims priority to British Patent Application No. GB1719520 , filed November 24, 2017 . Status of the Claims Claims 1-13 are currently pending. Claim Objections Claim 13 is objected to because of the following informalities: at line 1 the claim recites “wherein method comprises.” This phrase appears to lack a definite article (“the”) before the word “method,” and should seemingly read, “wherein the method comprises.” Appropriate correction is required. Claim Rejections - 35 USC § 112 (b) 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. Claim 7 is indefinite : Claim 7 is 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 7 is indefinite for reciting, “wherein said CPP sequence is selected from the group comprising or consisting of…,” because this defines an improper Markush group. In particular, a Markush group generally cannot use the open transition, “comprising,” as this makes it impossible to reasonably determine what the limits of the Markush group are. Abbott Labs v. Baxter Pharmaceutical Products, Inc. , 334 F.3d 1274, 1280 (Fed. Cir. 2003 ). See also MPEP 2173.05(h)I. Claim Rejections - 35 USC § 112(a) The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. Claims 1- 13 fail to comply with the written description requirement : Claims 1- 13 are rejected under 35 U.S.C. § 112, first paragraph, as failing to comply with the written description requirement. The claims contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventors, at the time the application was filed, had possession of the claimed invention. Specifically, Applicant does not have written description support for a method of treating one or both of a neurodegenerative or neuropsychiatric disorder, the method comprising administering to a patient to be treated an effective amount of a peptide comprising a neuroprotective peptide sequence for inhibiting Mitogen-activated protein kinase 3 (MAPK3) protein kinase signaling comprising an amino acid sequence sharing at least 75% identity with the peptide of SEQ ID NO:1. As discussed further below, the examples of the instant specification involve, and demonstrate efficacy in conferring a neuroprotective effect, using peptides having the full identity with the peptide of SEQ ID NO:1. Furthermore, the art indicates that a small number of mutations can potentially have a dramatic effect on the biological function of a peptide. As such, the present claims lack sufficient written description. The written description requirement is distinct from the enablement requirement; as was first pointed out by the court in In re Ruschig , 3 79 F .2d 990, 154 USPQ 118 (CCP A 1967), and clarified in Vas-Cath Inc. v. Mahurkar , 935 F.2d 1555, 19 USPQ2d 1111 (Fed. Cir. 1991). The issue of whether the claimed subject matter is adequately supported/described by the specification, is a question of fact. Id. at 1563, 19 USPQ2d at 1116. When considering whether the claimed subject matter complies with the written description requirement, Applicants' disclosure should be read in light of the knowledge possessed by those skilled in the art. "[T]he disclosure in question must be read in light of the knowledge possessed by those skilled in the art, and that knowledge can be established by affidavits of fact composed by an expert, and by referencing to patents and publications available to the public ... " In re Lange , 644 F.2d 856, 863, 209 USPQ 288, 294. See also, In re Alton , 76 F.3d 1168, 37 USPQ2d 1578 (Fed. Cir. 1996). Applicants enjoy the presumption that their patent application is valid and all statements contained therein are accurate; it is the PTO's burden to demonstrate why any of Applicants claims should be rejected or why any of Applicant's statements should be doubted. "it is incumbent upon the Patent Office, whenever a rejection ... is made, to explain why it doubts the truth or accuracy of any statement in a supporting disclosure and to back up assertions of its own with acceptable evidence or reasoning which is inconsistent with the contested statement. Otherwise, there would be no need for the applicant to go to the trouble and expense of supporting his presumptively accurate disclosure." In re Marzocchi , 439 F.2d 220, 224, 169 USPQ 367, 370. If successful in presenting such evidence and argument, the burden then shifts to the Applicant to provide evidence that would convince one to the contrary. The Invention in General A component of Applicant’s invention relates to a peptide comprising a neuroprotective peptide sequence for inhibiting Mitogen-activated protein kinase 3 (MAPK3) protein kinase signaling, having an amino acid sequence QGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDV (SEQ ID NO:1), and referred to as RB5. The disclosure teaches that this peptide sequence , by inhibiting MAPK3 in the cytoplasm, induces MAPK3 to translocate to the nucleus, resulting in enhanced MAPK3-mediated gene transcription and chromatin remodeling, particularly in the brain. In related aspects, the peptide can be associated with a peptide carrier, such as a cell penetrating peptide (CPP) acting to facilitate membrane translocation In related aspects, the invention relates to nucleic acid molecules (or vectors containing such nucleic acids) encoding the aforementioned peptide. In additional aspects, the invention relates to methods for treating or preventing a neurodegenerative disorder, the methods comprising administering an aforementioned peptide, nucleic acid, or vector to a patient in need of such treatment. The Claimed Invention The claimed invention is directed to a method of treating a neurodegenerative or neuropsychiatric disorder (or both). The method comprises administering to a patient in need of treatment an effective amount of at least one of the following: ( i ) peptide comprising RB5; (ii) a peptide comprising a sequence having at least 75% identity with RB5; (iii) a nucleic acid molecule encoding peptide ( i ) or (ii); (iv) a vector containing nucleic acid molecule (iii); or a pharmaceutical composition containing any of the aforementioned. In its broadest sense, then, claim 1 requires administration of (A) a peptide having at least 75% identity to RB5 or (B) a nucleic acid molecule encoding such a peptide. Dependent claims recite higher percentages of required identity to RB5 (claim 2) or that the peptide further comprises a peptide carrier covalently or non-covalently bound to it (claim 3). Additional dependent claims specify the nature of the peptide carrier, including its means of attachment, the identity of the disorder to be treated, and the route of administration. The Supporting Disclosure Applicants' supporting disclosure describes the peptide RB5, and its various uses, compositions, combinations, etc . (pgs. 4-18). This description is combined with definitions of various terms . A primary conclusion presented by the disclosure, a conclusion which forms a foundation of the claimed subject matter, is that peptides derived from the N-terminal domain of MAPK3 (MAPK3 is alternatively referred to as ERK1) promote selective activation of nuclear ERK signaling (see paragraph [0008]). In particular, the disclosure suggests that such a peptide, of which RB5 is an example, inhibits MAPK3 in the cytosol, thereby promoting MAPK3 translocation to the nucleus, where the nuclear MAPK3 thus . The data supporting these conclusions is largely presented in the drawings, described at pgs. 18-24. Figure 1 shows that RB selectively stimulates nuclear ERK signaling The drawings of the disclosure (described at pg. 18-24) provide, inter alia , data showing ERK2 activation by RB5 but not by SCR (an RB5 analog peptide having the same amino acid composition as RB5, but with a scrambled (“SCR”) sequence ). Other drawings illustrate data showing that this effect is enhanced by inclusion of a cell penetrating peptide (CPP) sequence . All testing occurred with one of four peptides: RB5, SCR , CCP-RB5, and CCP-SCR (noting that RB5 having an associated CCP is occasionally referred to as RB5-TA T (e.g. Fig. 13), where TAT refers to the HIV Trans-Activator of Transcription peptide) . Thus, and importantly, whereas the instant claims encompass the use of peptides having as little as 75% sequence identity to RB5 (i.e. 8 of 32 amino acids can be substituted), the specification only discloses evidence of the effectiveness of RB5 itself, with no amino acid substitutions. The State of the Art A number of references establish that moderately high sequence identity (such as 75%) is no assurance of conserved function, particularly in small peptides. These references further establish that small amino acid sequence variations, particularly in critical residues, can markedly alter or abolish biological function. For example, the non-patent publication, Glucagon-Like Peptide-1 and Its Class B G Protein–Coupled Receptors: A Long March to Therapeutic Successes , Pharmacol . Rev. , 6 8 , pgs. 954-1013 (20 16 ) by Graaf et al. (hereinafter, “ Graaf ”) reviews state-of-the-art findings on the structure and function of GLP-1, a n ~ 30 amino acid alpha-helical peptide (Abstract , Fig. 2). Among other things, Graaf collates the results of various mutagenesis studies of GLP-1 (pg. 964, D. Mutagenesis), amounting to alanine scanning mutagenesis in which various residues across the peptide are replaced with alanine. For example, Graaf teaches that, Point substitution of Phe28, Ile29, and Leu32 residues into Ala all had a significant negative impact on GLP-1–binding affinity and potency, confirming the important role of this hydrophobic region I in the C terminus of GLP-1 in binding the ECD of GLP-1R [] . The effect of substitution on binding affinity (GLP-1 radioligand competition IC50) and potency (cAMP activity EC50) was, however, much larger for Phe28 (1300/1000-fold decrease in affinity/potency) and Ile29 (93/27-fold reduction) compared with Leu32 (17/twofold decrease), indicating that interactions of Phe28 and Ile29 with the conserved hydrophobic core of the ECD of GLP-1R are particularly important [] . Substitution of Ala24 by Arg (the corresponding residue in glucagon) did not affect GLP-1 affinity, whereas Val33Ala (glucagon mimicking) and Ala30Gln mutations only had a moderate 5- to 6-fold effect on GLP-1 affinity [] . - Graaf , pg s . 965-966 , a. GLP-1 hydrophobic region I Graaf further teaches that, Substitution of Val16, Tyr19, and Leu20 into Ala decreased GLP-1 affinity by six-fold (Val16, Leu20) to 19-fold (Tyr19), and had similar negative effects on potency ( Adelhorst et al., 1994), showing that Tyr19 in particular is an important interaction site in hydrophobic region II located in the middle of the GLP-1 α-helix. - Graaf , pg . 966 , b. GLP-1 hydrophobic region II Graaf further teaches that, Replacement of Asp15 by Ala resulted in a 41-fold decrease in affinity and loss of potency [] ) … Replacement of Glu21 by Ala and Gly significantly decreased GLP-1 affinity by 15-fold and 60-fold, respectively ( Adelhorst et al., 1994; Watanabe et al., 1994), indicating that the side chain of Glu21 plays a key role in GLP-1 binding. Glu27Ala substitution had a moderate sixfold effect on binding affinity, but a greater, 240-fold, effect on potency, albeit with a large S.E.M. in the EC50 of the mutant [] . - Graaf , pg . 966 , c. Polar residues in α -helix Graaf further teaches that, Alanine substitution of Thr11, Phe12, and Thr13, the three residues in GLP-1 that are proposed to stabilize the N-capped conformation [] of the N terminus of GLP-1, had a significant impact on ligand affinity. The effect of the Thr11Ala substitution was, however, smaller (13-fold decrease) compared with Phe12Ala and Thr13Ala substitutions (133-fold decrease), whereas GLP-1 potency was only significantly affected by the latter two substitutions. - Graaf , pg . 966 , d. N-capping motif in GLP-1 Graaf further teaches that, Substitution studies indicate that the electrostatic, steric, and conformational properties of the four residues following the N-capping motif of GLP-1 (His7, Ala8, Glu9, Gly10) are important determinants for GLP-1R binding and/or activation. - Graaf , pg . 966 , e. N terminus of GLP-1 These studies indicate that, in the context of the 37 aa GLP-1, at a substantial number of positions, a single point mutation will cause a moderate-to-severe loss in biological function. Similarly, the non-patent publication, Identification of Key Residues for Interaction of Vasoactive Intestinal Peptide with Human VPAC 1 and VPAC 2 Receptors and Development of a Highly Selective VPAC 1 Receptor Agonist , J. Biol. Chem. , 275 , pgs. 24003-24012 (2000) by Nicole et al. (hereinafter, “ Nicole ”) teaches alanine scanning mutagenesis of vasoactive intestinal peptide (VIP – see Abstract ), a prominent neuropeptide with wide distribution in the peripheral and central nervous systems, having a wide range of biological actions in mammals (pg. 24003, first sentence). The data show that substituting residues at 14 positions out of 28 in VIP resulted in a >10-fold increase of K i or EC 50 at the VPAC 1 receptor (Abstract, and Table 1). Above: Table 1 of Nicole Thus, about half of the positions in the 28 aa VIP peptide are sufficiently sensitive to alanine substitution to result in substantial loss of biological effect. Again, these represent only single- point substitutions with alanine , generally considered a relatively conservative mutation (loss of side chain) . Other point mutations are frequently more deleterious, such as charge inversions, introduction of bulky side chains, are hydrophobic/hydrophilic inversions. See, for example, the non-patent publication, The Exchangeability of Amino Acids in Proteins , Genetics , 170 , pgs. 1459-1472 (2005) by Yampolsky et al., noting, inter alia , that alanine is on average the most tolerated replacement amino acid in a substitution mutation ( e.g. T A, K A, etc., see pg. 1465, left column, first full paragraph , and Table 3 ), with other substitutions such as T W being substantially more deleterious, on average (Table 3). Furthermore, while the above teachings relate to single point mutations, multiple point mutations would tend to cumulatively increase the likelihood of deleterious effects and loss of biological activity. See, for example, the non-patent publication, Optimization of the antimicrobial peptide Bac7 by deep mutational scanning , BMC Biology , 20 , art. no. 114 pgs. 1-21 (2022) by Koch et al., which teaches that, when substituting multiple amino acid residues in proteins or peptides, the effect on function usually equals the sum of the effect of the single substitutions (additive effects; see pg. 6, left column, Effects of amino acid residue combinations , first paragraph). Thus, a homolog of instant RB5 having eight mutations (out of 32 residues in RB5, thus 75% identity to RB5) would be likely to have substantially degraded or altered biological effect, and therefore likely to be ineffective in the method of instant claim 1. Summary of Written Description Rejection In view of the findings described above, the disclosure does not reasonably support the breadth of claim 1 . Claim 1 recites a method of treating a neurodegenerative or psychiatric disorder comprising, in the broadest version, administering a peptide comprising 75% identity with the 32mer peptide, RB5. However, the specification only discloses testing, and demonstration of likely efficacy in the method, of RB5 itself (or RB5 coupled with an additional peptide). Further, the teachings of the art indicate that a mutated variant of a ~30mer peptide, having only 75% identity with the wild type (25% substituted positions) is likely to have substantially degraded or nonexistent biological function. In view of this incongruity between the claimed breadth and the disclosed data, in light of the teachings of the art, claim 1 and its dependent claims, 2-13, fail to comply with the written description requirement. 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 1-13 are rejected for nonstatutory double patenting over the ’502 patent : Claims 1-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 1-7 of U.S. Patent No. 11,471,502 (hereinafter, “ the ’502 patent ”) . Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are directed to a method of use of a compound/composition (RB5 and compositions containing it), while the reference patent claims the compound itself, and discloses the presently claimed methods of use . Claim 1 of the ’502 patent is directed to the RB5 peptide of the instant claims. Claims 2-7 of the ’502 patent are directed to nucleic acids encoding RB5, pharmaceutical compositions containing the peptide and/or the nucleic acid, and a method for enhancing cognitive ability comprising administering the peptide or nucleic acid. The methods of the instant claims 1-2 and 9-13 are obvious variations of the method of claim 7 of the ’502 patent , particularly as modified by the composition claims 1-6 of the ’502 patent . Furthermore, t he Federal Circuit, and its predecessor court, has repeatedly held that a use of a composition can be obvious for nonstatutory double patenting rejections in view of claims directed to the composition itself in a reference patent, particularly where the specification of the reference application discloses the use claimed in the subject application. See, for example, In re Byck , 48 F.2d 665, 666 (CCPA 1931) , where the Court stated that [ i ] t would shock one’s sense of justice if an inventor could receive a patent upon a composition of matter, setting out at length in the specification the useful purposes of such composition, manufacture and sell it to the public, and then prevent the public from making any beneficial use of such product by securing patents upon each of the uses to which it may be adapted. In the present case, RB5 and its compositions are claimed in the ’502 patent , and the methods of the instant claims are directly disclosed in the ’502 patent . A s such, a finding of nonstatutory double patenting is appropriate. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to ALEXANDER K SHOWALTER whose telephone number is (571)270-0610. The examiner can normally be reached M-F 9:00 am to 5:00 pm, eastern time. 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Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /ALEXANDER K. SHOWALTER/ Examiner, Art Unit 1629 /JEFFREY S LUNDGREN/ Supervisory Patent Examiner, Art Unit 1629