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 .
Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
Response to Arguments
Applicant’s arguments filed 10/10/2025 with respect to rejections of claims 1, 5, 7, and 8 under 35 U.S.C. 102(a)(1)/(a)(2) have been fully considered and are persuasive. The rejections have been withdrawn.
Applicant's arguments filed 10/10/2025 with respect to rejection of claims 1, 5, 7-8, 13-16, and 23-24 under 35 U.S.C. 103 have been fully considered but they are not persuasive.
Applicants submit that 1) one of ordinary skill in the art would not have been motivated to combine the Eliasson and Walensky and 2) the structurally-stabilized stapled peptides of the claimed methods demonstrate unexpected properties in terms of their ability to selectively target certain bacterial and/or cancerous cells over others.
Regarding 1), Eliasson provides motivation to combine. Eliasson teaches that magainin II has both lytic activity against bacterial species as well as cancer species ([0004, 0006, 0036]), which is common theme among antimicrobial peptides; Cruciani further evidences the inherent lytic properties of magainin II against cancerous cells. Moreover, Eliasson further teaches that structure-activity studies carried out with magainins have shown that enhancement of helicity and of cationic charge leads to higher antibacterial activity (see [0006]). As the relationship between magainin II and its ability to lyse both bacterial and cancerous cells has already been established, it follows that improvements to the peptide that augment its ability to lyse one type of cell should similarly improve its ability to lyse the other type of cell. In this case, one would reasonably expect that improving the ability of magainin II to lyse bacterial cells would similarly improve its ability to lyse cancerous cells as well.
Moreover, knowing that improvement of magainin II through further stabilizing its helical structure and cationic charge would lead one to Walensky, who teaches both improvements; SEQ ID NO: 43 of Walensky (instant SEQ ID NO: 60) exhibits both increased helical stability through peptide stapling and cationic charge with the substitution of multiple residues for Lys. Thus, one skilled in the art would have indeed have motivation to combine Eliasson and Walensky as well as a reasonable expectation of success given that the ability of magainin II to lyse both bacterial and cancerous cells was established in the art.
Regarding 2), MPEP 716.02(b)(I) states that the burden is on the Applicant to establish that the results are unexpected and significant: “The evidence relied upon should establish "that the differences in results are in fact unexpected and unobvious and of both statistical and practical significance." Ex parte Gelles, 22 USPQ2d 1318, 1319 (Bd. Pat. App. & Inter. 1992).” In the instant application, none of the data put forth demonstrate statistical significance, including Examples 3 and 5 and Figures 9, 26, and 27, as cited in arguments. Thus, this requirement has not been met.
Moreover, MPEP 716.02(d) requires that unexpected results be commensurate in scope with the claimed invention: “Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In other words, the showing of unexpected results must be reviewed to see if the results occur over the entire claimed range.”
The claims of the instant application are drawn to a method of killing cancer cells and/or treating cancer in humans through administration of a structurally-stabilized peptide 18-50 amino acids in length and with at least 65% identity over the full-length to SEQ ID NO: 1 or any of SEQ ID NO: 219-221, 228, 231, and 232. The data in the instant application demonstrate that some species as claimed, such as SEQ ID NO: 2, 17, and 60, can exert cancer-cell specific or tunable effects (Figures 18-27). However, the data does not support unexpected results commensurate in scope with the claimed invention as it is clear that not all stapled peptides contained with the genera of claims 1 and/or 5 possess these unexpected properties; additionally, no evidence of unexpected results have been demonstrated with respect to SEQ ID NO: 219-221, 228, 231, and 232. Although in some instances unexpected results of a species may be sufficient to overcome an obviousness rejection so long as one skilled in the art could reasonably determine a trend in the exemplified data that would allow them to extrapolate the results (see MPEP 716.02(d)(I)), in the instant case there is no throughline or trend that one skilled in the art would be able to reasonably use to extrapolate therefrom. Consequently, the arguments set forth are insufficient to overcome the outstanding obviousness rejection, which has been maintained/modified herein.
Applicant's arguments filed 10/10/2025 with respect to rejection of claims 1, 5, 7-8, 13-16, and 23-24 for double patenting have been fully considered but they are not persuasive for the same reasoning stated above.
Regarding the IDS’s submitted previously, see IDS section below.
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1, 5, 7, 8, 13-16, 23, and 24, drawn to a method of treating cancer with a structurally-stabilized peptide in the reply filed on 6/13/2025 is acknowledged.
Claim Status
Claims 1, 5, 7-8, 13-16, 24, 29-31, 35, 37, 40-41, 47, and 59-69 are pending. Claims 29-31, 35, 37, 40-41, 47 and 59 were previously withdrawn as non-elected inventions. Claims 62, 63, 67, and 68 are hereby withdrawn as non-elected species. Claims 1, 5, 8, and 13 are currently amended. Claims 60-69 are new. Claims 7, 14-16, and 24 were previously presented. Claims 2-4, 6, 9-12, 17-23, 25-28, 32-34, 36, 38-39, 42-46, and 48-58 are cancelled.
Priority
The instant application is the 371 national stage entry of PCT/US2020/065078, filed 12/15/2020, which claims priority to the provisional application 62/948,582, filed 12/16/2019. The priority date of 12/16/2019 is acknowledged.
Information Disclosure Statement
Applicant correctly noted that the IDS submitted on 6/13/2025 had not been considered. All references therein are under consideration here and a copy attached.
Moreover, Applicant requested an explanation as to why some references on the IDS submitted on 12/6/2022 had not been considered. In the prior Office Action, the Examiner did not discover the references in the file wrapper; however, reevaluation of the file wrapper for the current Office Action uncovered the references previously not considered. They are now under consideration and a modified annotated copy of the IDS from 12/6/2022 has been attached.
Please note that the information provided in both the IDS submitted 6/13/2025 and 12/6/2022 does not materially change the previous Office Action.
Claim Objections
Claim 64 is objected to because of the following informalities: the claim recites “a lunch cancer cell” in line 9. Per the instant specification, a lunch cancer cell is being interpreted as a lung cancer cell. Appropriate correction is required.
Maintained/Modified - Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, 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 text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
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.
Claim(s) 1, 5, 7, 8, 13-16, 24, 60, 61, 64-66, and 69 are rejected under 35 U.S.C. 103 as being unpatentable over Eliasson et al. (US 20080019993 A1, filed 3/21/2007, published 1/24/2008), as evidenced by Cruciani et al. (Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3792-6.), and Walensky (WO 2019/018499 A2, filed 7/18/2018, published 1/24/2019, on IDS filed 12/6/2022).
Eliasson teaches cytotoxic peptides with three or more cationic residues that have one or more generally-bulky and lipophilic amino acids as well as pharmaceutical compositions and their uses as antibacterial or antitumoral agents (Abstract). Eliasson teaches a method of treating cancer in a subject in need of such treatment wherein the method comprises administering to the subject an effective amount of a lytic compound wherein the lytic compound, through lysis of cells in a first tumour, generates an immune response which inhibits tumor cell formation or growth of a second tumour ([0010, 0144]). The subject may be any human or non-human animal, preferably a mammal, more preferably a human ([0162]). Preferably the lytic compound is a peptide ([0164]).
Eliasson also teaches a method of treating tumours in a patient comprising the administration of one or more of the peptides of the invention ([0113]; claim 37). The patient can be an animal or human ([0053]).
The peptides taught by Eliasson are derivatives of the antibacterial peptide magainin II (“Mag2” or SEQ ID NO: 28), which are known to lyse bacteria ([0004, 0297, 0331]; Sequence Listing Pg 39). SEQ ID NO: 28 of Eliasson and the instant SEQ ID NO: 1 are identical. As evidenced by Cruciani, magainin II is capable of selectively lysing cancer cells while leaving normal cells intact (Pg 3792, “Magainins are cytotoxic for various tumor cells” and “Magainins are selectively cytotoxic for tumor cells”, left column; Figure 1; Table 1).
Eliasson does not teach that SEQ ID NO: 28/the instant SEQ ID NO: 1 is a structurally-stabilized stapled peptide.
Walensky teaches methods of generating and optimizing stabilized (e.g., stapled and/or stitched) anti-microbial peptides (StAMPs) for the prophylaxis and treatment of antibiotic-resistant (e.g., colistin-resistant, methicillin resistant, meropenem-resistant) bacterial infections
(e.g., Gram-negative, Gram-positive), and methods for using such peptides (Abstract). Walensky teaches many peptides derived from well-known and established antimicrobial peptides, including from magainin II. SEQ ID NO: 43 of Walensky is one example of a magainin II-derived antimicrobial peptide that has been structurally-stabilized via peptide staples (Pg 66, Table 1, wherein X residues can be a number of non-natural amino acids used in the creation of peptide staples). SEQ ID NO: 43 is 23 amino acids in length, identical to the instant SEQ ID NO: 60, and displays >65% sequence identity to the instant SEQ ID NO: 1, as shown below:
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124
590
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Thus, regarding claims 1 and 5, Eliasson teaches methods of killing or inhibiting a cancer cell and treating cancer in a human subject in need thereof comprising administering an effective amount of the peptide magainin II that has the ability to lyse cancer cells. Walensky teaches an improved version of magainin II, the peptide SEQ ID NO: 43, in which the X residues can be any non-natural amino acid involved in a stapling procedure, thereby stabilizing the alpha-helical structure of the peptide and improving its efficacy. Therefore, it would be prima facie obvious to use the improved magainin II peptide, SEQ ID NO: 43 taught by Walensky, in a method of lysing cancer cells or treating cancer as taught by Eliasson, to increase the potency of the peptide and improve the efficacy of the treatment. One skilled in the art would have a reasonable expectation of success as it was already established that magainin II without any structural modifications or further stabilization through stapled peptides could effectively lyse cancerous cells and treat cancer.
Regarding claims 7 and 8, Eliasson further teaches that the tumor to be treated can be selected from the group consisting of lymphomas, carcinomas and sarcomas, most preferably B-cell lymphoma ([0160]; Figure 11 and [0185]).
Regarding claims 13, 24, 60, 64-66, and 69, Walensky teaches the structurally-stabilized peptide SEQ ID NO: 43 consists of the sequence GXGKFXHSKKKFGKAXVGEXAKK (Table 1, Pg 67). The X residues can be the same or different; non-natural amino acids comprising olefinic side chains; both selected from the group consisting of (S)-2-(4-pentenyl)Ala-OH, (R)-2-(4-pentenyl)Ala-OH, (R)-2-(7-
octeny1)Ala-OH, (S)-2-(7-octeny1)Ala-OH and 2-amino-2-(pent-4-eny 1 )hept-6-enoic
acid, (R)-2-(2-propenyl)Ala-OH, (S)-2-(2-propenyl)Ala-OH. In certain embodiments,
if a sequence has two "X's" both X's are (S)-2-(4-pentenyl)Ala-OH. In certain
embodiments, if a sequence has two "X's" both X's are (R)-2-(4-pentenyl)Ala-OH.
In certain embodiments, if a sequence has two "X's" both X's are (R)-2-(7-
octenyl)Ala-OH. In certain embodiments, if a sequence has two "X's" both X's are
(S)-2-(7-octenyl)Ala-OH. In certain embodiments, if a sequence has two "X's" both
X's are 2-amino-2-(pent-4-enyl)hept-6-enoic acid. In certain embodiments, if a
20 sequence has two "X's" both X's are (R)-2-(2-propenyl)Ala-OH. In certain
embodiments, if a sequence has two "X's" both X's are (R)-2-(2-propenyl)Ala-OH.
In certain embodiments, if a sequence has two "X's" both X's are (S)-2-(2-
propenyl)Ala-OH. In certain embodiments, if a sequence has two "X's" both X's are
different non-natural amino acids and can, e.g., be selected from the group consisting of S)-2-(4-pentenyl)Ala-OH, (R)-2-(4-pentenyl)Ala-OH, (R)-2-(7-octenyl)Ala-OH,
(S)-2-(7-octenyl)Ala-OH, 2-amino-2-(pent-4-enyl)hept-6-enoic acid, (R)-2-(2-
propenyl)Ala-OH, and (S)-2-(2-propenyl)Ala-OH. In certain instances, if the two
X's are separated by 3 amino acids, the two X's can be different non-natural residues,
5 e.g, the first Xis (R)-2-(2-propenyl)Ala-OH or (S)-2-(2-propenyl)Ala-OH and the
second Xis (S)-2-(2-propenyl)Ala-OH or (R)-2-(2-propenyl)Ala-OH. In certain instances, the “X’s” can be any residue/substance that permits formation of a staple and/or stitch; permits formation of a hydrocarbon staple and/or stitch; lactam stapled; triazole stapled; stapled using UV-cycloaddition staple; disulfide stapled; oxime stapled; tioesther stapled; photoswitcable staple; double-click stapled; bis-lactam stapled; or comprise a bis-arylation staple (Pg 67, line 2 through 69, line 21). As disclosed in the instant specification, the X residues of the elected/instant SEQ ID NO: 60 can also be any of the above non-natural amino acids capable of forming a stapled peptide (“any stapling amino acid”; Pg 88, line10 – Pg 89, line 20 of instant specification).
Regarding claim 14, Walensky teaches Formula I shown below:
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276
500
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, or a pharmaceutically acceptable salt thereof, wherein: each R1 and R2 is independently H, alkyl, alkenyl, alkynyl, arylalkyl, cycloalkylalkyl, heteroarylalkyl, or heterocyclylalkyl, any of which is substituted or unsubstituted; each R3 is independently alkylene, alkenylene, or alkynylene, any of which is substituted or unsubstituted; each x is independently 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10; each w and y is independently 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20; z is 1, 2, 3, 4, 5, 6, 7, 8, 9,or 10; and each Xaa is independently an amino acid, wherein the StAMP exhibits an antimicrobial effect against at least one microbe, and wherein the [Xaa]w and/or [Xaa]y of the StAMP comprises at least one hydrophobic patch of two or more hydrophobic amino acids that is identical to a hydrophobic patch present on an anti-microbial peptide (AMP) that is identical to the StAMP of Formula I except that at least one of the two or more hydrophobic amino acids of the hydrophobic patch of the StAMP is substituted with an amino acid having reduced hydrophobicity; and/or the StAMP comprises an amino acid substitution that alters the charge nature of a cationic point charge relative an anti-microbial peptide (AMP) that is identical to the StAMP of Formula I (Pg 48, line 25 – Pg 49, line 24).
The term "alkyl" refers to a hydrocarbon chain that may be a straight chain or branched chain, containing the indicated number of carbon atoms. For example, C1-C10 indicates that the group may have from 1 to 10 (inclusive) carbon atoms in it. In the absence of any numerical designation, "alkyl" is a chain (straight or branched) having 1 to 20 (inclusive) carbon atoms in it. The term "alkylene" refers to a divalent alkyl (i.e., -R-) (Pg 124, lines 13-18).
Figure 4 of Walensky indicates that one StAMP is StAMP51 2.0, which is also known as Mag(i+4)1,15(A9K,B21A,N22K,S23K), or SEQ ID NO: 43. Because the instant SEQ ID NO: 60 and SEQ ID NO: 43 of Walensky are the same, Walensky reads upon the instant claim 14, option (v) wherein each [Xaa]w is GX1GKFX2HSKKKFGKA (SEQ ID NO:97), each [Xaa]x is VGE, and each [Xaa]y is AKK, wherein each of X1 and X2 is a stapling amino acid as described above, and wherein a side chain of X1 is cross-linked to a side chain of X2.
Regarding claims 15 and 16, Walensky teaches that in certain instances, the “X” residues can both be (R)- or (S)-2-(4-pentenyl)Ala-OH, which meets the limitations wherein R1 and R2 are both methyl (an alkyl) and R3 is -CH2-CH2-CH2-CH=CH-CH2-CH2-CH2- (an alkenyl; Pg 7, lines 18-20). Walensky also teaches that in certain instances, the “X” residues can both be (R)- or (S)-2-(7-octenyl)Ala-OH, which meets the limitations wherein R1 and R2 are both methyl (an alkyl) and R3 is -(CH2)6-CH=CH(CH2)6- (an alkenyl).
Regarding claim 61, Eliasson teaches that peptides of the invention can be used to treat leukemia (Figure 7; [0310]).
Maintained/Modified - 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, 5, 7, 8, 13-16, 24, 60, 61, 64-66, and 69 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 8, 9, 11, 12 and 15-16 of U.S. Patent No. 10,464,975 ('975) in view of Eliasson et al. (US 20080019993 A1, filed 3/21/2007, published 1/24/2008) as evidenced by as evidenced by Cruciani et al. (Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3792-6.). 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 U.S. Patent No. ‘975 recites a therapeutic compound comprising a cross-linked amino acid sequence having the formula:
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272
825
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or a pharmaceutically acceptable salt thereof, wherein:
each R1 and R2 is independently H, alkyl, alkenyl, alkynyl, arylalkyl, cycloalkylalkyl, heteroarylalkyl, or heterocyclylalkyl, any of which is substituted or unsubstituted; each R3 is independently alkylene, alkenylene, or alkynylene, any of which is substituted or unsubstituted; each x is 3 or 6; each w and y is independently 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20; z is 1, 2, 3, or 4; and each Xaa is independently an amino acid, wherein the cross-linked amino acid sequence has 3, 4, 5, 6, 7, 8 or 9 amino acid substitutions relative to the sequence set forth in SEQ ID NO:3; wherein the substitutions are:(a) two or more amino acid substitutions with stapling amino acids that are internally cross-linked; and (b) one or more of: (i) a substitution with a basic amino acid; (ii) a substitution with a histidine; (iii) a substitution with a D-alanine; (iv) a substitution with an alanine; and (v) a substitution of a methionine with a norleucine; wherein at least one of the substitutions of (b) is selected from the group consisting of: (i) a substitution with a lysine at position 9 of SEQ ID NO:3; (ii) a substitution with a histidine, and (iii) a substitution with a glutamic acid; wherein the cross-linked amino acid sequence has an alpha helical conformation; and wherein the compound exhibits an increased antibacterial effect against at least one bacterium relative to an un-cross-linked corresponding sequence set forth in SEQ ID NO:3.
SEQ ID NO: 3 is magainin II. The instant SEQ ID NO: 60 of the present application meets the above limitations as it has 8 total substitutions relative to SEQ ID NO: 3 of U.S. Patent No. ‘975, including four X residues that are involved in internal cross-linking and an alanine to lysine substitution at position 9. SEQ ID NO: 60 is described as having a helical confirmation (see instant specification, Figures 9 and 11).
Dependent claims include the compound of claim 1, wherein R3 is C8 alkylene, C8 alkenylene, or C8 alkynylene; the sum of x, w, and y is at least 10; and z is 1 or 2 (claim 2); the compound of claim 1, wherein R3 spans from one to two turns on an α-helix (claim 3); the compound of claim 1, wherein the R3 is substituted by dihydroxylation and/or aminohydroxylation (claim 8); the compound of claim 1, wherein z=1 (claim 9); a pharmaceutical composition comprising the compound of claim 10 (claim 11); a pharmaceutical composition comprising the therapeutic compound of claim 1 (claim 12); the therapeutic compound of claim 1, wherein the stapling amino acid is an α,α-disubstituted amino acid (claim 15); the therapeutic compound of claim 1, wherein the stapling amino acid is S5 [(S)-2-(4-pentenyl)Alanine] or R5 [(R)-2-(4-pentenyl)Alanine] (claim 16).
U.S. Patent No. ‘975 does not teach the described therapeutic compound is used in a method of treating cancer comprising administering to a human patient in need thereof an effective amount of the peptide that specifically lyses cancer cells.
As referenced above, Eliasson teaches cytotoxic peptides, pharmaceutical compositions, and their uses as antibacterial or antitumoral agents. More specifically, Eliasson teaches a method of treating cancer in a subject in need of such treatment wherein the method comprises administering to the subject an effective amount of a lytic compound wherein the lytic compound, through lysis of cells in a first tumour, generates an immune response which inhibits tumor cell formation or growth of a second tumour. Preferably the lytic compound is a peptide and the subject is human. Eliasson also teaches a method of treating tumours in a patient comprising the administration of one or more of the peptides of the invention. One lytic compound/peptide taught by Eliasson is the antibacterial peptide magainin II, which can kill Meth A cells derived from fibrosarcoma. As evidenced by Cruciani, magainin II can specifically lyse cancer cells while leaving normal cells intact. Additional types of cancer that can be treated using this method include lymphomas, carcinomas, most preferably B-cell lymphoma.
It would have been prima facie obvious to one of ordinary skill in the art to incorporate the teachings of U.S. Patent No. ‘975 into the method taught by Eliasson thereby arriving at the instant invention. One would have a reasonable expectation of success as Eliasson established that magainin II could lyse cancerous cells. Thus, the above claims are referend obvious in light of the teachings of U.S. Patent No. ‘975.
Claims 1, 5, 7, 8, 13-16, 24, 60, 61, 64-66, and 69 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. Patent No. 11,325,955 ('955) in view of Eliasson et al. (US 20080019993 A1, filed 3/21/2007, published 1/24/2008) as evidenced by as evidenced by Cruciani et al. (Cruciani RA, Barker JL, Zasloff M, Chen HC, Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3792-6.). 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 U.S. Patent No. ‘955 recites a stapled peptide or pharmaceutically acceptable salt thereof comprising the amino acid sequence: GX1GKFX2HSKKKFGKAX3VGEX4AKK (SEQ ID NO:43), wherein each of X1, X2, X3, and X4 is a non-natural amino acid; wherein X1 and X2 are cross-linked to each other; and wherein X3 and X4 are cross-linked to each other.
Dependent claims include the stapled peptide or pharmaceutically acceptable salt thereof of claim 1, wherein each of X1, X2, X3, and X4 is independently an α, α-disubstituted non-natural amino acid comprising an olefinic side chain (claim 2); the stapled peptide or pharmaceutically acceptable salt thereof of claim 1, wherein each of X1, X2, X3, and X4 is (S)-2-(4-pentenyl)Ala-OH (claim 3); a pharmaceutical composition comprising the stapled peptide or pharmaceutically acceptable salt thereof of claim 3, and a pharmaceutically acceptable carrier (claim 4); the stapled peptide or pharmaceutically acceptable salt thereof of claim 1, wherein the stapled peptide is between 23 and 30 amino acids in length, inclusive (claim 5); a pharmaceutical composition comprising the stapled peptide or pharmaceutically acceptable salt thereof of claim 1, and a pharmaceutically acceptable carrier (claim 6).
U.S. Patent No. ‘955 does not teach that SEQ ID NO: 43 is used in a method of treating cancer comprising administering to a human patient in need thereof an effective amount of the peptide that specifically lyses cancer cells.
As referenced above, Eliasson teaches cytotoxic peptides, pharmaceutical compositions, and their uses as antibacterial or antitumoral agents. More specifically, Eliasson teaches a method of treating cancer in a subject in need of such treatment wherein the method comprises administering to the subject an effective amount of a lytic compound wherein the lytic compound, through lysis of cells in a first tumour, generates an immune response which inhibits tumor cell formation or growth of a second tumour. Preferably the lytic compound is a peptide and the subject is human. Eliasson also teaches a method of treating tumours in a patient comprising the administration of one or more of the peptides of the invention. One lytic compound/peptide taught by Eliasson is the antibacterial peptide magainin II, which can kill Meth A cells derived from fibrosarcoma. As evidenced by Cruciani, magainin II can specifically lyse cancer cells while leaving normal cells intact. Additional types of cancer that can be treated using this method include lymphomas, carcinomas, most preferably B-cell lymphoma.
It would have been prima facie obvious to one of ordinary skill in the art to incorporate the teachings of U.S. Patent No. ‘955 into the method taught by Eliasson thereby arriving at the instant invention. One would have a reasonable expectation of success as Eliasson established that magainin II could lyse cancerous cells. Thus, the above claims are referend obvious in light of the teachings of U.S. Patent No. ‘955.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa L Fisher can be reached at 571-270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/FRED H REYNOLDS/Primary Examiner, Art Unit 1658
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