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 .
Response to Amendment
Applicant’s amendment filed 08/13/2026 is acknowledged. Claim 1 is amended. Claims 16-19, 21, 25-34, 39 and 41 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. In the Remarks filed 02/16/2026, Applicant originally elected the species of “CNSHTQGKC”, corresponding to SEQ ID NO: 3 with a C residue added at either end (see Table 1 at pages 32-33) and the examiner extended the search to include SEQ ID NO: 1. Applicant’s amendment has deleted reference to SEQ ID NO: 1, therefore, the search will be extended to include SEQ ID NOs: 4 and 8.
Claims 1-3, 6, 8, 10 and 11 are under examination.
Objections/Rejections Withdrawn
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim Objections
The objection to claim 1 for minor informalities is withdrawn in response to Applicant’s amendment correcting the grammatical error.
Claim Rejections - 35 USC § 112(a) – Scope of Enablement
The rejection of claims 1-3, 6, 8 and 10 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph for scope of enablement is withdrawn in response to Applicant’s amendment of the claims to be limited to a 7-mer peptide sequence selected from SEQ ID NOs: 3-5, 8 and 9. The claims no longer encompass peptides sharing only 30% identity to the recited sequences.
Claim Rejections - 35 USC § 112(a) – Written Description
The rejection of claims 1-3, 6, 8 and 10 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112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in response to Applicant’s amendment of the claims to be limited to a 7-mer peptide sequence selected from SEQ ID NOs: 3-5, 8 and 9. The claims no longer encompass peptides sharing only 30% identity to the recited sequences.
Claim Rejections - 35 USC § 102
Claims 1-3, 6, 10 and 11 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Leissring (WO 2019/055431—on IDS filed 12/16/2024) is withdrawn in response to Applicant’s amendment of claim 1 to delete reference to SEQ ID NO: 1. Leissring does not teach the currently recited peptides.
Claim Rejections - 35 USC § 103
The rejection of claims 1-3, 6, 8, 10 and 11 under 35 U.S.C. 103 as being unpatentable over Peng et al. (ChemRxiv (2019) 1-54) in view of Fominaya et al. (Ther. Deliv. (2015)(6)(10): 1171-1194) is withdrawn upon further consideration. Specifically, Applicant’s argument at pages 7-8 that the charge attribute, net charge, PI, molecular weight and hydropathy score cannot be used to identify any particular peptide sequence is persuasive.
Rejections Maintained
Claim Rejections - 35 USC § 112(a)
Scope of Enablement
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.
The rejection of claim 11 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph for scope of enablement is maintained for reasons of record and the following. The specification, while enabling for the claimed peptides comprising a sequence selected from SEQ ID NOs: 3, 4 and 8, does not reasonably provide enablement for the claims as broadly recited. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims. Though claim 11 is now limited to SEQ ID NOs: 3-5, 8 and 9, it still encompasses peptides having residues ranging from 8-25 residues in length, which encompass peptides having up to a 70% difference between the encompassed peptides and the sequences disclosed in the instant specification.
The rejection at pages 4-8 of the Office action mailed 05/13/2026, which sets forth the issues regarding the breadth and unpredictability of the encompassed peptides, is as follows:
The claims encompass peptides having 7-25 amino acid residues comprising a sequence selected from SEQ ID NOs: 1-20, and these peptides may be linked to a therapeutic or diagnostic payload (see claims 1, 8 and 10). The specification discloses twenty 7mer peptides in Table 1, which notes that SEQ ID NOs: 1-20 with N- and C-terminal flanking cysteine (C) residues were also tested (see pages 32-33). The instant claims, however, are broad with respect to the recited peptides, which encompass peptides having up to 25 residues, and not just the 7- and 9mers disclosed in the instant specification. This represents up to a 70% difference between the encompassed peptides and the sequences disclosed in the instant specification.
When considering enablement of a claimed peptide, it is appropriate to consider its intended use. The instant specification discloses that the “therapeutic or diagnostic payload” is carried across the blood-brain barrier (BBB) comprising administering one of the peptides of the invention (see p. 3, lines 23-27). The experimental portion of the instant specification discloses that Pep-3 (i.e., SEQ ID NO: 3) most effectively crossed the BBB and into the parenchyma of the brain in vivo (see p. 39, lines 11-26). The post-filing date art of Peng et al. (Bioconjugate Chem. 2023, 34, 2319-2336—on IDS filed 12/16/2024) confirm these data, noting that Pep-3 “traverse[d] the BBB and enter[ed] the brain parenchyma” and “demonstrated effective brain distribution” (see p. 2330, left column, 2nd and 3rd paragraphs). These data were also published in the preprint publication by Peng et al. in ChemRxiv (2019) 1-54, published 12 June 2019 (see paragraph bridging pages 30-31 and p. 33, 2nd paragraph). The specification does not teach how the peptides may contain up to 18 additional amino acid residues while maintaining the ability to carry therapeutic or diagnostic payloads across the BBB.
The instant specification discloses that a small number of the twenty disclosed peptides were capable of crossing the BBB. Applicant does not teach how the peptides may be mutated by up to 70% via the addition of amino acid residues of while still resulting in peptides capable of crossing the BBB. The art recognizes that mutations can be destabilizing and their effects unpredictable. Peng et al. teach “any type of modification to the BBB-shuttling peptides may influence the binding or recognition of the peptides to the targets on the brain capillary endothelium, and work involving therapeutic carriers such as nanoparticles will have to take this into consideration when measuring BBB transport” (see p. 2330, right column, 1st paragraph).
Although machine learning algorithms have improved the ability to predict protein 3D structure from sequences, methods based on artificial intelligence for predicting the impact of mutations on protein stability still face challenges, including prediction biases towards “generalization”, “data set”, “destabilizing mutations” and the inability to predict the effects of multiple mutations. See Figure 1, at p. 162 and the discussion at pages 165-166 of Pucci et al. (Current Opinion in Structural Biology 2022, 72: 161-168). Even in the case of single mutations, artificial intelligence programs do not accurately “predict the impact of mutation on protein stability” or function (see p. 2, 2nd paragraph and p. 7, 1st full paragraph of Pak et al., PLoS ONE 18(3): e0282689. https://doi.org/10.1371/ journal.pone.0282689).
In the instant case, the claims encompass up to a 70% divergence from SEQ ID NOs: 1 and 3, which in practical terms constitutes an addition of up to 18 amino acid residues. Applicants have provided little or no guidance beyond the mere presentation of sequence data to enable one of ordinary skill in the art to determine, without undue experimentation, the positions in the protein which are tolerant to change by amino acid substitutions or deletions, and the nature and extent of changes that can be made in these positions. Although the specification outlines art-recognized procedures for producing and screening for active muteins, this is not adequate guidance as to the nature of active derivatives that may be constructed, but is merely an invitation to the artisan to use the current invention as a starting point for further experimentation. This is borne out by Applicant’s own data, which shows that only a small number of the tested peptides were capable of crossing the BBB into the parenchyma of the brain in vivo.
Due to the large quantity of experimentation necessary to generate and test the encompassed peptides for the ability to carry a therapeutic or diagnostic payload across the BBB, the lack of direction/guidance presented in the specification regarding peptides other than those disclosed at Table 1 of the instant specification, the absence of working examples directed to peptides containing more than 9 residues, the complex nature of the invention, the unpredictability of the effects of mutation on peptide structure and function, and the breadth of the claims which fail to recite limitations on the peptides, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope.
Response to Arguments
Applicant argues at p. 5 that the claims are now limited to 7-mer peptides selected from SEQ ID NOs: 3, 4, 5, 8 and 9.
This argument has been fully considered but is not found persuasive. Claim 11 still encompasses 8-25mer peptides, and therefore, still encompasses peptides having up to 70% divergence from SEQ ID NOs: 3-5, 8 and 9.
Written Description
The rejection of claim 11 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 is maintained for reasons of record and the following. Though claim 11 is now limited to SEQ ID NOs: 3-5, 8 and 9, it still encompasses peptides having residues ranging from 8-25 residues in length, which encompass peptides having up to a 70% difference between the encompassed peptides and the sequences disclosed in the instant specification.
The rejection at pages 8-10 of the Office action mailed 05/13/2026, which sets forth the issues regarding the lack of written description of the encompassed peptides, is as follows:
The claims encompass peptides having 7-25 amino acid residues comprising a sequence selected from SEQ ID NOs: 1-20, and these peptides may be linked to a therapeutic or diagnostic payload (see claims 1, 8 and 10). Therefore, the claims encompass peptides capable of carrying either therapeutic or diagnostic payloads to cells. The claims also recite that the peptides may contain between 7-25 amino acid residues. To provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof.
In deciding whether the application complies with the written description requirement of 35 USC 112(a) or 35 USC 112 (pre-AIA ), first paragraph, it is necessary to understand what Applicant has possession of and what Applicant is claiming. From the specification, it is clear that Applicant has possession of twenty 7mer peptides, and teaches the 7mer peptides may be flanked and the N- and C-termini with cysteine (C), abbreviated in the specification as “CX7C peptides” (see Table 1 at pages 32-33). The experimental portion of the instant specification discloses that Pep-3 (i.e., SEQ ID NO: 3) most effectively crossed the BBB and into the parenchyma of the brain in vivo (see p. 39, lines 11-26). The instant specification discloses that a small number of the twenty disclosed peptides were capable of crossing the BBB, and that these peptides contained 7 amino acid residues. The post-filing date art of Peng et al. (Bioconjugate Chem. 2023, 34, 2319-2336) confirm these data, noting at that Pep-3 “traverse the BBB and enter the brain parenchyma” and “demonstrated effective brain distribution” (see p. 2330, left column, 2nd and 3rd paragraphs). These data were also published in the preprint publication by Peng et al. in ChemRxiv (2019) 1-54, published 12 June 2019 (see paragraph bridging pages 30-31 and p. 33, 2nd paragraph).
The specification does not teach, however, how the peptides may contain up to 18 additional amino acid residues, which is equivalent to mutating the sequences by up to 70%, while maintaining the ability to carry therapeutic or diagnostic payloads. Peng et al. teach “any type of modification to the BBB-shuttling peptides may influence the binding or recognition of the peptides to the targets on the brain capillary endothelium, and work involving therapeutic carriers such as nanoparticles will have to take this into consideration when measuring BBB transport” (see p. 2330, right column, 1st paragraph). Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). With the exception of SEQ ID NOs: 1-20, the skilled artisan cannot envision the detailed chemical structure of the encompassed peptides, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Therefore, only peptides comprising the amino acid sequence set forth in SEQ ID NOs: 1-20, but not the full breadth of the claim meets the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Response to Arguments
Applicant argues at p. 5 that the claims are now limited to 7-mer peptides selected from SEQ ID NOs: 3, 4, 5, 8 and 9.
This argument has been fully considered but is not found persuasive. Claim 11 still encompasses 8-25mer peptides, and therefore, still encompasses peptides having up to 70% divergence from SEQ ID NOs: 3-5, 8 and 9.
New Rejections
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 11 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. This rejection was necessitated by Applicant’s amendment.
Claim 11 depends upon claim 1 and recites that the peptide “is 8-25 residues in length, 9-25 residues in length, 10-25 residues in length, 12-25 residues in length, 15-25 residues in length or 20-25 residues in length”. Claim 1 has been amended to recite a 7-mer peptide sequence, therefore, claim 11 is now broader in scope than and fails to further limit the claim upon which it depends. Applicant may cancel the claim, amend the claim to place it in proper dependent form, rewrite the claim in independent form, or present a sufficient showing that the dependent claim complies with the statutory requirements.
Notice for all US Patent Applications filed on or after March 16, 2013: 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.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 6, 8 and 10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rezende Vaz et al. (BR102017026076, published 04/28/2020; translation provided by Orbit Express via the Scientific & Technical Information Center. This rejection was necessitated by Applicant’s amendment. Rezende Vaz et al. teach a peptide, NWMINKE (SEQ ID NO: 13), which is an Annexin A1 inhibitor peptide that can be used in the treatment of breast cancer (see claims 1-2). The sequence alignment between SEQ ID NO: 13 of Rezende Vaz et al. and instant SEQ ID NO: 8 is as follows:
RESULT 1
BHS23327
ID BHS23327 standard; peptide; 7 AA.
AC BHS23327;
DT 11-JUN-2020 (first entry)
DE Annexin A1 inhibitor peptide, SEQ ID 13.
KW Annexin A1 inhibitor; breast tumor; cell signaling; cytostatic;
KW endocrine-gen.; gynecological; protein inhibition; protein therapy;
KW therapeutic.
OS Unidentified.
CC PN BR102017026076-A2.
CC PD 28-APR-2020.
CC PF 04-DEC-2017; 2017BR-10026076.
PR 04-DEC-2017; 2017BR-10026076.
CC PA (UYUB-) UNIV FEDERAL UBERLANDIA.
CC PA (FAPE-) FAPEMIG FUNDACAO AMPARO A PESQUISA DO ES.
CC PI Goulart Filho LR, Alves Pereira Zoia M, Van Petten De Vasconcelos;
CC PI Vaz ER, Lara V, De Almeida Araujo Santos F;
DR WPI; 2020-44020H/046.
CC PT Annexin A1 inhibitor peptide used in the treatment of triple negative
CC PT breast cancer and other diseases that depend on Annexin A1 to develop,
CC PT has seven, eight amino acids.
CC PS Claim 1; SEQ ID NO 13; 30pp; Portuguese.
CC The present invention relates to a novel Annexin A1 inhibitor peptide of
CC SEQ ID NO:1-15 (see BHS23315-BHS23329) and their reverse sequences of SEQ
CC ID NO:16-30 (see BHS23331-BHS23345) used in the treatment of triple
CC negative breast cancer and other diseases that depend on Annexin A1 to
CC develop. The invention also provides an immunogenic composition
CC comprising the Annexin A1 inhibitor peptide and their reverse sequences.
CC The annexin A1 inhibitor peptide of the invention promotes the inhibition
CC of signaling of this oncoprotein.
SQ Sequence 7 AA;
Query Match 100.0%; Score 42; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 NWMINKE 7
|||||||
Db 1 NWMINKE 7
Rezende Vaz et al. teach that the peptides may comprise a non-amino acid chemical feature, polyethylene glycol, and/or be conjugated to diagnostic or therapeutic payloads (see claims 5-10). Thus, Rezende Vaz et al. teach the limitations of claims 1, 6, 8 and 10.
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 factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-3, 6, 8, 10 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Choi et al. (Translation of KR20170061333 provided by the Korean Ministry of Intellectual Property, which is the application document of KR2018127561, published 11/29/2018) in view of Fominaya et al. (Ther. Deliv. (2015)(6)(10): 1171-1194—of record). This rejection was necessitated by Applicant’s amendment. The first factor to consider when making a rejection under 35 U.S.C. 103(a) is to determine the scope and contents of the prior art. Choi et al. teach a 7-mer peptide having the sequence TYLNSAK that binds toll-like receptor 2 (see Figure 8), which shares 100% sequence identity with instant SEQ ID NO: 4:
Query Match 100.0%; Score 35; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 TYLNSAK 7
|||||||
Db 1 TYLNSAK 7
The object of the invention of Choi et al. is to device a process of screening for peptides that bind porcine TLR-2 that may be useful in vaccine delivery (i.e., therapeutic payload; see claim 1; paragraph [0002] of the translation). While Choi et al. teach another peptide binds TLR-2 more strongly, TYLNSAK is still among one of the five peptides identified in the biopanning process (see Figure 8), thus, one having ordinary skill in the art would be choosing from a limited number of peptides that bind TLR-2. A known or obvious composition does not become patentable simply because it has been described as somewhat inferior to some other product for the same use.
The second factor to consider is to ascertain the differences between the prior art. Choi et al. do not teach the peptide contains D-amino acids or non-amino acid chemical features as recited in claims 2, 3, 6 or 10 or a diagnostic payload as recited in claim 8. Regarding linking peptides to a non-natural amino acid, a D-amino acid or an non-amino acid chemical feature such as PEG, Fominaya et al. teach that cell-penetrating peptides, defined therein as short peptides that can cross cell membranes, have attributes that are useful for many “in vivo applications”, including delivering vaccines (see p. 1172, left column, 2nd paragraph). Nevertheless, peptides are inherently unstable in vivo, thus Fominaya et al. discuss various techniques for increasing stability and half-life, including using non-natural amino acids, D-amino acids and PEGylation (see p. p. 1177, left column, 1st and 2nd paragraphs; p. 1178-1179 under “Non-natural amino acids”; pages 1183-1184 under “Polymer conjugation”). Note that linking the peptide in Choi et al. with a non-natural amino acid would also result in an 8-mer peptide, which would meet the limitation of claim 11.
It would have been obvious to the person of ordinary skill in the art at the time of the filing of the invention to modify the peptides taught in Choi et al. by linkage to a non-natural amino acid or PEG or substitution with a D-amino acid because the prior art of Fominaya et al. recognized these were well-established techniques for increasing stability, bioavailability and half-life of cell penetrating peptides (see p. 1172, bottom of right column). The person of ordinary skill in the art would have been motivated to make these modifications because peptides are often unstable, and there is an art-recognized need to extend their half-life. Furthermore, the person of ordinary skill in the art could have reasonably expected success because these protein modifications were well-known in the art.
Thus, the claims do not contribute anything non-obvious over the prior art.
Claims 1-3, 6, 8, 10 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Rezende Vaz et al. (BR102017026076, published 04/28/2020; translation provided by Orbit Express via the Scientific & Technical Information Center in view of Fominaya et al. (Ther. Deliv. (2015)(6)(10): 1171-1194—of record). This rejection was necessitated by Applicant’s amendment. The first factor to consider when making a rejection under 35 U.S.C. 103(a) is to determine the scope and contents of the prior art. Rezende Vaz et al. teach a peptide, NWMINKE (SEQ ID NO: 13), which is an Annexin A1 inhibitor peptide that can be used in the treatment of breast cancer (see claims 1-2). The sequence alignment between SEQ ID NO: 13 of Rezende Vaz et al. and instant SEQ ID NO: 8 is as follows:
RESULT 1
BHS23327
ID BHS23327 standard; peptide; 7 AA.
AC BHS23327;
DT 11-JUN-2020 (first entry)
DE Annexin A1 inhibitor peptide, SEQ ID 13.
KW Annexin A1 inhibitor; breast tumor; cell signaling; cytostatic;
KW endocrine-gen.; gynecological; protein inhibition; protein therapy;
KW therapeutic.
OS Unidentified.
CC PN BR102017026076-A2.
CC PD 28-APR-2020.
CC PF 04-DEC-2017; 2017BR-10026076.
PR 04-DEC-2017; 2017BR-10026076.
CC PA (UYUB-) UNIV FEDERAL UBERLANDIA.
CC PA (FAPE-) FAPEMIG FUNDACAO AMPARO A PESQUISA DO ES.
CC PI Goulart Filho LR, Alves Pereira Zoia M, Van Petten De Vasconcelos;
CC PI Vaz ER, Lara V, De Almeida Araujo Santos F;
DR WPI; 2020-44020H/046.
CC PT Annexin A1 inhibitor peptide used in the treatment of triple negative
CC PT breast cancer and other diseases that depend on Annexin A1 to develop,
CC PT has seven, eight amino acids.
CC PS Claim 1; SEQ ID NO 13; 30pp; Portuguese.
CC The present invention relates to a novel Annexin A1 inhibitor peptide of
CC SEQ ID NO:1-15 (see BHS23315-BHS23329) and their reverse sequences of SEQ
CC ID NO:16-30 (see BHS23331-BHS23345) used in the treatment of triple
CC negative breast cancer and other diseases that depend on Annexin A1 to
CC develop. The invention also provides an immunogenic composition
CC comprising the Annexin A1 inhibitor peptide and their reverse sequences.
CC The annexin A1 inhibitor peptide of the invention promotes the inhibition
CC of signaling of this oncoprotein.
SQ Sequence 7 AA;
Query Match 100.0%; Score 42; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 NWMINKE 7
|||||||
Db 1 NWMINKE 7
Rezende Vaz et al. teach that the peptides may comprise polyethylene glycol or be conjugated to diagnostic or therapeutic payloads (see claims 5-10).
The second factor to consider is to ascertain the differences between the prior art. Rezende Vaz et al. do not teach the peptide contains D-amino acids or non-natural amino acids. Regarding linking peptides to a non-natural amino acid or substituting D-amino acids, Fominaya et al. teach that cell-penetrating peptides, defined therein as short peptides that can cross cell membranes, have attributes that are useful for many therapeutic applications (see p. 1172, left column, 2nd paragraph). Nevertheless, peptides are inherently unstable, thus Fominaya et al. discuss various techniques for increasing stability and half-life, including using non-natural amino acids and D-amino acids (see p. p. 1177, left column, 1st and 2nd paragraphs; p. 1178-1179 under “Non-natural amino acids”; pages 1183-1184 under “Polymer conjugation”). Note that linking the peptide taught by Rezende Vaz and colleagues with a non-natural amino acid would also result in an 8-mer peptide, which would meet the limitation of claim 11.
It would have been obvious to the person of ordinary skill in the art at the time of the filing of the invention to modify the peptides taught in Rezende Vaz et al. by linkage to a non-natural amino acid or substitution with a D-amino acid because the prior art of Fominaya et al. recognized these were well-established techniques for increasing stability, bioavailability and half-life of cell penetrating peptides (see p. 1172, bottom of right column). The person of ordinary skill in the art would have been motivated to make these modifications because peptides are often unstable in vivo, and there is an art-recognized need to extend their half-life. Furthermore, the person of ordinary skill in the art could have reasonably expected success because these protein modifications were well-known in the art.
Thus, the claims do not contribute anything non-obvious over the prior art.
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 CHRISTINA M BORGEEST whose telephone number is (571)272-4482. The examiner can normally be reached M-F 9-5:30 EDT.
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/CHRISTINA M BORGEEST/Primary Examiner, Art Unit 1675
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