DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant's election with traverse of Group I, claims 1-12, drawn to a compound comprising a peptide having the structure of Formula I, in addition to the species of a PKCε inhibitor, in the reply filed on 11/17/20205 is acknowledged. The traversal is on the ground(s) that 1) a lack of unity of invention has not been shown as Johnson does not teach a compound of Formula I and 2) no rationale was provided for the species election requirement. This is not found persuasive.
First and most importantly, as stated in the prior Restriction/Election requirement, a national stage application containing claims to different categories of invention will be considered to have unity of invention if the claims are drawn only to one of the following combinations of categories (1)-(5), as provided in 37 CRF 1.475(b) (see Restriction/Election requirement, Pg 4-5). The inventions as listed in Groups I-III do not constitute a combination of categories of inventions in accordance with 37 CFR 1.475(b) because the claims are drawn to two products (Groups I and II) and one process of use (Group III). Therefore, the claims are not drawn only to one of the combinations of categories and, thus, lack unity of invention. This is sufficient to break unity of invention and unity of species.
Regarding 1) and 2), these points are moot given that unity of invention was first and foremost broken based upon the fact that the instant claims do not meet the requirements of 37 CRF 1.475(b).
The requirement is still deemed proper and is therefore made FINAL.
Claim Status
Claims 1-20 are pending. Claims 7-9 and 13-20 are hereby withdrawn as non-elected inventions (claims 13-20) and species (claims 7-9). Claim 1 is currently amended.
Priority
The instant application is the 371 national stage entry of PCT/US2021/023943, filed 3/24/2021, which claims priority to provisional applications 63017488, filed 4/29/2020, and 62994098, filed 3/24/2020. The priority date of 3/24/2020 is acknowledged.
Information Disclosure Statement
The IDS filed on 9/23/2022 is under consideration.
Claim Objections
Claims 1, 4, and 10 are objected to because of the following informalities:
Claims 1 and 10 recite a “peptide haying the structure” or “a peptide haying an amino acid sequence”, respectively.
Claim 4 recites that TAT has an amino acid sequence identical to or at least about 80% identity to any one of SEQ ID NO: 1-3. The Sequence Listing indicates that SEQ ID NO: 2 and SEQ ID NO: 3 are identical.
Appropriate correction is required.
Claim Interpretation
Regarding the objections to claims 1 and 10 above, for purposes of examination, the claims will be interpreted as a peptide having the structure or an amino acid sequence (emphasis added).
Claims 3, 4, 6, and 10-12 each recite variations of limitations wherein a component of Formula I “…has an amino acid sequence…” (emphasis added). This claim is being interpreted as a peptide comprising the component of Formula I, wherein a peptide or protein encompassing or containing the entirety of the component of Formula I meets the limitation of the claim. Conversely, smaller fragments encompassed by the component of Formula I (i.e., dipeptides) are being interpreted as not meeting the limitations of the claim.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-6 and 10 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 1 recites a compound comprising a peptide with the structure of Formula I, Myr-TAT-L-P, wherein, with the exception of Myr, each of the components TAT, L, and P are all peptide sequences. The scope of this claim is indefinite because where each peptide component starts and stops (the boundaries of each of the peptide components) is unclear. Without a clearly defined sequence for each of these components, how would one skilled in the art know where the TAT module ends and the linker begins? Or where the linker ends and the PKC modulator begins? For purposes of examination, the claim is being interpreted based upon the TAT, L, and P sequences delineated in claims 3, 4, 6, and 10.
Further, by virtue of their dependency on claim 1, claims 2 and 5 are also rejected for this same reasoning.
Further, claim 3 recites that L has an amino acid sequence identical to or with at least about 80% identity to any one of SEQ ID NOS: 9-14. The scope of this claim is indefinite as it is unclear whether the amino acid sequence of L can indeed be ~80% of any of SEQ ID NO: 9-14 or must be identical to one of them. Claims 4, 6, and 10 recite similar language regarding the amino acid sequences of TAT (claim 4), PKCε (claim 6), and TAT, L, and PKCε (claim 10), and, thus, are also rejected here for this same reasoning.
For purposes of examination, the claims are being interpreted where an amino acid sequence with at least about 80% sequence identity meet the limitations of the claims.
Further, claim 10 recites the limitation "the peptide modulator of PKCε" in line 2. There is insufficient antecedent basis for this limitation in the claim as there is no prior recitation of a peptide modulator of PKCε in parent claim 1, only a peptide modulator of PKC.
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 1-5 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) 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 inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The claims are drawn to a compound comprising Formula I, Myr-TAT-L-P, wherein Myr is myristoyl, TAT is the transduction domain of Trans-Activator of Transcription or lipidated adducts thereof, L is a linker peptide, and P is a peptide modular of PKC. The rejection stems from the limitation “P is a peptide modulator of PKC,” which recites a feature by functional rather than structural language. There is nothing further in the claim to indicate the structural feature(s) (i.e., an amino acid sequence(s)) required to meet this functional limitation, and describing an invention by function is insufficient to meet the written description requirement.
Per MPEP 2163(II)(3)(a), for some biomolecules, examples of identifying characteristics include a sequence, structure, binding affinity, binding specificity, molecular weight, and length. Although structural formulas provide a convenient method of demonstrating possession of specific molecules, other identifying characteristics or combinations of characteristics may demonstrate the requisite possession. As explained by the Federal Circuit, "(1) examples are not necessary to support the adequacy of a written description; (2) the written description standard may be met … even where actual reduction to practice of an invention is absent; and (3) there is no per se rule that an adequate written description of an invention that involves a biological macromolecule must contain a recitation of known structure." Falkner v. Inglis, 448 F.3d 1357, 1366, 79 USPQ2d 1001, 1007 (Fed. Cir. 2006); see also Capon v. Eshhar, 418 F.3d at 1358, 76 USPQ2d at 1084 ("The Board erred in holding that the specifications do not meet the written description requirement because they do not reiterate the structure or formula or chemical name for the nucleotide sequences of the claimed chimeric genes" where the genes were novel combinations of known DNA segments.). However, the claimed invention itself must be adequately described in the written disclosure and/or the drawings. For example, disclosure of an antigen fully characterized by its structure, formula, chemical name, physical properties, or deposit in a public depository does not, without more, provide an adequate written description of an antibody claimed by its binding affinity to that antigen, even when preparation of such an antibody is routine and conventional. See Amgen Inc. v. Sanofi, 872 F.3d 1367, 1378, 124 USPQ2d 1354, 1361 (Fed. Cir. 2017)("knowledge of the chemical structure of an antigen [does not give] the required kind of structure-identifying information about the corresponding antibodies"); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1351-52, 97 USPQ2d 1870, 1877 (Fed. Cir. 2011)(patent disclosed the antigen the claimed antibody was supposed to bind, but did not disclose any antibodies with the specific claimed properties).
Brandman et al. (Peptides derived from the C2 domain of protein kinase C epsilon (epsilon PKC) modulate epsilon PKC activity and identify potential protein-protein interaction surfaces. J Biol Chem. 2007 Feb 9;282(6):4113-23.) describes the process of identifying peptide modulators of PKCε. In their study, Brandman focused on identifying peptide modulators derived from the C2 domain of PKCε because their previous work uncovered both a peptide activator and a peptide inhibitor from this same region. Brandman wanted to further evaluate the C2 domain of PKCε through a peptide-scanning method to determine if other peptide modulators could be identified and characterized (Abstract; Pg 4119, Discussion, right column, first paragraph). In total, Brandman identified 13 peptide modulators that either activated or inhibited PKCε through its C2 domain (Figure 1 and Table 1).
Brandman also notes that because the 3D structure of the C2 domain from other PKC isozymes is structurally similar, peptide modulators derived from homologous positions in other PKC isozymes will likely have similar biological activities. Brandman predicts that many other peptide modulators will be derived from the C2 domains of other PKC isozymes (Pg 4121, Discussion, right column, second paragraph).
However, these few examples do not accurately capture the breadth of the claims. In addition to the peptide modulators taught by Brandman, which are specific to PKCε, there are an additional 9 other known PCK isozymes, each of which is composed of multiple domains that interact with one or more binding partners, such as receptors and substrates, to effect function; moreover, PCK isozymes also utilize intramolecular interactions for regulatory purposes (see Figure 1 and 2 and Pg 4, final paragraph – Pg 5, first paragraph of Churchill. Rationally designed peptide regulators of protein kinase C. Trends Endocrinol Metab. 2009 Jan;20(1):25-33.). Peptides designed to target any of these domains or isozymes that modulate, either by increasing or decreasing, PCK activity, to any degree, would also qualify as peptide modulators per the limitations of the instant claims.
Thus, based on the lack of structural limitations recited, a peptide that modulates any of the interactions between any given domain of any PKC isozyme and an interacting partner would meet the limitations of the instant claims. Thus, the claim effectively reads on any peptide so long as it can modulate any PKC isozyme in any way, shape, or form.
Applicants have disclosed the peptide modulators of PKC can include both inhibitors and activators that act on isozymes ε, βII, ζ and δ, and the species SEQ ID NO: 4-8 are specifically claimed. No other examples are disclosed within the instant specification, and the claims listed above are written such that they contemplate or include additional compounds that retain the same functional characteristics beyond these limited examples. Thus, the instant specification does not provide adequate written description to possess the broad genus described above.
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.
Claim(s) 1-6 and 10-12 are rejected under 35 U.S.C. 103 as being unpatentable over Johnson et al. (US 2010/0311671 A1, published 12/9/2010; cited on IDS filed 9/23/2022), as evidenced by Chen et al. (protein linkers: property, design and functionality. Adv Drug Deliv Rev. 2013 Oct;65(10):1357-69.).
Johnson teaches methods for transdermal delivery of PKC modulatory peptides (Abstract). The PKC modulatory peptide can be modified by attachment to another peptide or to a linker to form a fusion peptide or a conjugate. As an example, the peptide modulator may be linked or otherwise conjugated to a second peptide by an amide bond from the C-terminal of one peptide to the N-terminal of the other peptide. The peptide attached to the PKC modulatory peptide can be a peptide that functions to increase the cellular uptake of the peptide inhibitors, such as a CPP. One CPP contemplated by Johnson is Transactivating Regulatory Protein (TAT)-derived transport polypeptide ([0063, 0065]). The linker is an amino acid linker and can be, for instance, “GG” or any number of residues (2-8), where glycine is merely exemplary ([0067]).
Johnson states that examples and discussions herein that are particular to a specific PKC modulatory peptide are merely exemplary of the peptides for any given PKC isozyme. With this understanding, and based on the description above of exemplary cell penetrating peptides and approaches for linking to a PKC modulatory peptide, a skilled artisan can readily envision conjugates for use in the methods described herein. As an example, Johnson teaches SEQ ID NO: 14, which consists of the formula P-L-TAT, wherein P is a PKC peptide modulator, L is a peptide linker, and TAT is the CPP. The sequence of SEQ ID NO: 14 is EAVSLKPTGGYGRKKRRQRRR (Sequence Listing), wherein “EAVSLKPT” is a PKCε inhibitor identical to the instant SEQ ID NO: 4, “GG” is an amino acid linker L, and “YGRKKRRQRRR” is TAT identical to the instant SEQ ID NO: 1 ([0067]).
Johnson also teaches that PKC modulatory peptides or conjugates may be targeted by proteases in the body for degradation. One approach to protecting peptides from proteolytic degradation involves capping the amino and/or carboxy termini of the peptides, wherein capping refers to the introduction of a blocking group to the terminus via a covalent modification without decreasing the biological activity of the peptide. Acetylation of the amino termini is one method of protecting the peptides from proteolytic degradation but other capping moieties are also possible, including myristoyl ([0076]).
In summary, Johnson teaches a peptide conjugate of the general formula P-L-TAT that can be further modified by introducing a capping moiety, such as a myristoyl group, to the N-terminus of the peptide. Johnson does not explicitly teach a peptide conjugate of formula I, Myr-TAT-L-P.
However, it would have been prima facie obvious to try rearranging the relative order of TAT and P, thereby producing a compound of formula TAT-L-P. At the time of filing, the art recognized that connecting peptides or peptide domains to each other through linkers allowed the fusion protein to retain the individual structure and functionalities of the peptides or peptide domains, as evidenced by Chen (see Introduction, Pg1; 3.1 Flexible linkers, Pg 4-5). Moreover, Johnson also indicates that a skilled artisan can readily envision additional conjugates based upon the exemplary cell penetrating peptides and approaches for linking to a PKC modulatory peptide. One of ordinary skill in the art would recognize that a fusion peptide comprising two independent peptides/peptide domains connected by a single linker could only be combined in two different ways; moreover, one would recognize that after trying the orientation taught by Johnson, there would only be one other possible combination, the instant formula I as recited in claim 1. Therefore, it would be obvious to try this additional combination, based upon the teachings of Johnson as evidenced by Chen.
Moreover, per MPEP 2144.04(VI)(C), rearrangement of parts is one legal precedent recognized by the courts as directed to common practices that normally require only ordinary skill in the art and are considered routine expedients: “In re Japikse, 181 F.2d 1019, 86 USPQ 70 (CCPA 1950) (Claims to a hydraulic power press which read on the prior art except with regard to the position of the starting switch were held unpatentable because shifting the position of the starting switch would not have modified the operation of the device.); In re Kuhle, 526 F.2d 553, 188 USPQ 7 (CCPA 1975) (the particular placement of a contact in a conductivity measuring device was held to be an obvious matter of design choice).” In the instant case, the parts are TAT and P, which can easily be rearranged and connected by a single linker L to arrive at the instant formula I; Johnson teaches as much by disclosing that one skilled in the art can easily envision other protein conjugates that could be derived from the teachings at hand.
Further, Johnson teaches adding a lipid-based group to the N-terminus of such peptides in order to protect them from protein degradation; therefore, it would be obvious to further modify the peptide TAT-L-P by adding a myristoyl group to the N-terminus, thus producing the instant formula I. One skilled in the art would be motivated to do so in order to better protect the fusion peptide from protein degradation. One would have a reasonable expectation of success as Johnson established this as viable strategy to avoid protease activity.
Regarding claim 2, Johnson teaches that the peptide linker can be, for example, GG, but can be any number of residues, where glycine is merely exemplary ([0067]).
Regarding claim 3, Johnson does not explicitly teach any of the instant linkers SEQ ID NO: 9-14. However, as stated above, Johnson does teach that an amino acid linker can be, for instance, “GG” or any number of residues (2-8), where glycine is merely exemplary ([0067]). Moreover, Chen evidences that Gn, where n is the number of amino acids, is an ideal peptide linker based on its size and flexibility (Table 2 on Pg 29). Thus, it would be obvious to one skilled in the art to establish a peptide linker sequence of at least GGGG, thus rendering obvious the instant SEQ ID NO: 10.
Regarding claim 4, Johnson teaches the TAT protein sequence SEQ ID NO: 6, which is identical to the instant SEQ ID NO: 1 and exhibits >80% sequence identity to the instant SEQ ID NO: 2 and 3.
Regarding claim 5, Johnson teaches that PKC peptide modulators can include inhibitors of PKCε ([0048-0049]).
Regarding claim 6, Johnson teaches SEQ ID NO: 13 is an example of a PKCε inhibitory peptide, which is identical to the instant SEQ ID NO: 4 ([0049]; Sequence Listing).
Regarding claim 10, the rearrangement of the individual components of SEQ ID NO: 14 of Johnson (which consists of the instant SEQ ID NO: 4 (PKCε inhibitor), the linker GG, and SEQ ID NO: 1 (TAT)) with the addition of the N-terminal myristoyl group, renders the instant SEQ ID NO: 27 of claim 10 obvious. It also renders the instant SEQ ID NO: 18 obvious, which exhibits >80% sequence identity to the rearranged SEQ ID NO: 14 of Johnson.
Regarding claims 11 and 12, as stated above, Johnson teaches a protein sequence of TAT identical to the instant SEQ ID NO: 1, a linker peptide sequence identical to SEQ ID NO: 10, and a PKCε inhibitory peptide identical to SEQ ID NO: 4.
Claim(s) 1-6 and 10-12 are rejected under 35 U.S.C. 103 as being unpatentable over Mochly-Rosen et al. (US 20070066526 A1, published 3/22/2007; cited on IDS filed 9/23/2022) in view of Lindon (US 20070148628 A1, published 6/28/2007), as evidenced by Chen et al. (protein linkers: property, design and functionality. Adv Drug Deliv Rev. 2013 Oct;65(10):1357-69.).
Mochly-Rosen teaches a method for reducing risk of stroke in a subject with hypertension by administering an inhibitor of delta PKC to the subject (Abstract). Mochly-Rosen teaches that a therapeutically effective amount of the inhibitor is the quantity required to increase cerebral blood flow and/or reduce cell, tissue, or organ damage or death that occurs due to stroke and/or reperfusion following recanalization after and ischemic stroke ([0188]).
Mochly-Rosen also teaches Example 2 wherein rats were administered SEQ ID NO: 85, which is a TAT peptide identical to the instant SEQ ID NO: 1; SEQ ID NO: 87, which is a PKCε inhibitor identical to the instant SEQ ID NO: 4; or SEQ ID NO: 88, which is a conjugate thereof identical to the instant SEQ ID NO: 18 that mirrors “TAT-L-P” of the instant formula I, prior to induction of stroke ([0148]; Sequence Listing). Administration of SEQ ID NO: 88 improves the survival of rats after induction of stroke relative to saline or TAT alone (Figure 5).
Mochly-Rosen does not teach the addition of a myristoyl group to the N-terminus.
Lindon teaches solutions and peptides for preservation, perfusion, and/or reperfusion of an organ, especially the heart, for transplantation. The solution contains peptide inhibitor(s) of protein kinase C ε (PKC ε). Methods for using the inventive solution are also disclosed, including methods for protecting an ischemic organ from damage, for attenuating organ dysfunction after ischemia, for maintaining nitric oxide release and/or inhibiting superoxide release in an ischemic organ, and for protecting an organ from damage when isolated from the circulatory system (Abstract).
Lindon teaches that peptide PKCε inhibitors can be myristoylated at the N-terminus to further improve absorption into cells of the organ ([0020]).
Thus, regarding claim 1, Mochly-Rosen teaches a peptide conjugate comprising the formula TAT-L-P, wherein P is a PKCε peptide inhibitor. Lindon teaches that PKCε peptide inhibitors can be further improved by adding a myrstioyl group to the N-terminus of the peptide. Based on these teachings, it would be prima facie obvious to add the myristoyl group to the N-terminus of the peptide conjugate of general formula TAT-L-P taught by Mochly-Rosen. One skilled in the art would be motivated to do so in order to improve the absorption of the peptide taught by Mochly-Rosen into the cells of organs in need thereof. One would have a reasonable expectation of success as Lindon previously established that myristoylation of PKCε inhibitors improved their activity in methods of protecting organs after ischemic events.
Regarding claim 2, Mochly-Rosen teaches that the peptide linker can be, for example, CC, as exemplified in SEQ ID NO: 88.
Regarding claim 3, Mochly-Rosen does not explicitly teach any of the instant linkers SEQ ID NO: 9-14. However, it would be obvious to one skilled in the art to establish a peptide linker sequence of GGGG (instant SEQ ID NO: 10). One skilled in the art would recognize that the linker GGGG is a common linker made of flexible suitable for connecting different peptides or peptide domains that would preserve their individual functionality within a fusion protein, as evidenced by Chen.
Regarding claim 4, as stated above, Mochly-Rosen teaches the TAT protein sequence SEQ ID NO: 85, which is identical to the instant SEQ ID NO: 1 and exhibits >80% sequence identity to the instant SEQ ID NO: 2 and 3.
Regarding claims 5 and 6, as stated above, Mochly-Rosen teaches the PKC modulator can be a PKCε inhibitor such as SEQ ID NO: 87, which is identical to the instant SEQ ID NO: 4.
Regarding claims 10-12, as stated above, Mochly-Rosen teaches SEQ ID NO: 88 which is 100% identical to the instant SEQ ID NO: 18 and >80% identical to the instant SEQ ID NO: 27.
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 and 10-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 9 of U.S. Patent No. 8,084,195 B2 (US ‘195). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘195 recites a method for preserving an organ for transplantation, protecting an ischemic organ from damage, attenuating organ dysfunction after ischemia, maintaining nitric oxide release in an ischemic organ, or protecting an organ from damage after isolation from the circulatory system, said method comprising the step of perfusing the organ with a solution comprising at least one peptide inhibitor of protein kinase C βII (PKCβII), wherein the inhibitor of PKCβII is a peptide of 9 amino acids in length having SEQ ID NO: 1.
The instant claims recite a compound of Formula I which comprises a peptide modulator of PKC; the peptide modulator can be SEQ ID NO: 5, which is identical to SEQ ID NO: 1 of US ‘195. The instant specification teaches peptides of the invention can be used in methods for preserving an organ for transplantation, protecting an ischemic organ from damage, attenuating organ dysfunction after ischemia, and protecting an organ from damage after isolation from the circulatory system ([0011, 0054, 0055]).
Dependent claims include the at least one peptide inhibitor of PKCβII is myristoylated (claim 9).
Claims 1 and 10-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, and 9 of U.S. Patent No. 9,029,078 B2 (US ‘078). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘078 recites a method for preserving an organ for transplantation, protecting an ischemic organ from damage, attenuating organ dysfunction after ischemia, maintaining nitric oxide release in an ischemic organ, or protecting an organ from damage after isolation from the circulatory system, said method comprising the step of perfusing the organ with a solution comprising at least one peptide activator of protein kinase C δ (PKC δ).
The instant claims recite a compound of Formula I which comprises a peptide modulator of PKC, which can be an activator of PKC δ. The instant specification teaches peptides of the invention can be used in methods for preserving an organ for transplantation, protecting an ischemic organ from damage, attenuating organ dysfunction after ischemia, and protecting an organ from damage after isolation from the circulatory system ([0011, 0054, 0055]).
Dependent claims include species of the PKC δ activator (claim 4) and the peptide activator of PKC δ is myristoylated (claim 9).
Claims 1 and 10-12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, and 9 of U.S. Patent No. 9,462,803 B2 (US ‘803). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘803 recites a method for protecting an organ from reperfusion injury after ischemia, said method comprising the step of reperfusing the organ with a solution containing an inhibitor of protein kinase ε consisting of the amino acid sequence of SEQ ID NO: 1.
The instant claims recite a compound of Formula I which comprises a peptide modulator of PKC; the peptide modulator can be SEQ ID NO: 4, which is identical to SEQ ID NO: 1 of US ‘803. The instant specification teaches peptides of the invention can be used in a method of protecting an ischemic organ from damage ([0011, 0054, 0055]).
Dependent claims include the concentration of the PKCε inhibitor (claim 4) and SEQ ID NO: 1 is myristoylated (claim 9).
Prior Art Cited but not Referenced
MacLean et al. (US20090042769A1, published 2/12/2008; cited on IDS filed 9/23/2022) teaches methods to increase the stability and delivery efficiency of protein kinase C (PKC) modulatory peptide compositions (Abstract), peptide conjugates comprising TAT as a carrier protein (such as SEQ ID NO: 163, identical to the instant SEQ ID NO: 1) attached via a peptide linker to a PKCε inhibitor (such as SEQ ID NO: 83, identical to the instant SEQ ID NO: 4), and N-terminal acylation. MacLean does not teach N-terminal myristoylation. However, MacLean in view of Lindon, as evidenced by Chen, above, would render the instant claims 1-6 and 10-12 obvious.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sara E Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST.
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/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/FRED H REYNOLDS/Primary Examiner, Art Unit 1658