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/Restriction
Applicants’ election without traverse to prosecute the invention of Group I, claims 1-6 in the reply filed 19 February 2026 is acknowledged.
Claim 7 is withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention, there being no allowable generic or linking claim.
Status of Claims
The claim listing filed 19 February, 2026 is pending. Applicant’s election without traverse of Group I in the reply filed on 19 February, 2026 is acknowledged. Claims 4 and 6 have been canceled. Claims 8-14 have been added. Claims 13 and 14 are withdrawn as being drawn to a non-elected invention.
Claims 1-3, 5, and 8-12 are being examined on the merits in this office action.
Specification
Response to Arguments: The objections to the specification have been withdrawn in view of the amendments filed 19 February, 2026.
Claim Rejections - 35 USC § 112
Response to Arguments: The scope of enablement rejection of claim 4 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph has been withdrawn in view of the cancelation of claim 4 in the amendments filed 19 February 2026.
The scope of enablement rejection of claim 3 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph has been withdrawn in view of the amendments filed 19 February 2026.
The written description rejection of claims 1-6, under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph has been withdrawn in view of the amendments filed 19 February 2026.
The rejection of claims 4 and 6 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, for being indefinite has been withdrawn in view of the cancelation of claims 4 and 6 in the amendments filed 19 February 2026.
The following rejections are new as necessitated by the amendment filled 19 February 2026.
Claims 1-3, 5, 9, and 11 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 claimed invention is directed to a mimetic peptide that modulates connexin-46 by the mimetic peptide inhibiting an interaction between connexin-46 and c-Src, in an effort to decrease Akt activation and the stemness of cancer cells, comprising an amino acid sequence having at least 75% sequence similarity to the amino acid sequence set forth in SEQ ID NO: 4. The specification fails to disclose the what amino acids of SEQ ID NO: 4 can be changed, while maintaining the ability to inhibit an interaction between connexin-46 and c-Src. Applicant shows that the addition of 100mM of TAT-Cx46-Src to cellular media every 3 days resulted in reduced tumor sphere size in HeLa Cx46-GFP cells [FIG. 2(C)]. HeLa cells are currently used only as a model for cervical cancers, as Hela cells aren’t representative of all cancer types. HeLa cells cannot model the cellular diversity and specific characteristics only found in other cancer types.
There are no other structures, drawings, or teachings of other amino acid sequences described in the disclosure of a core structure that modulates connexin-46 interactions and has at least 75% sequence identical to SEQ ID NO: 4. There is no teaching of which 25% of the amino acid sequence of SEQ ID NO: 4 can vary and maintain the ability of modulating connexin-46 via inhibiting an interaction between connexin-46 and c-Src. The level of skill in the art is such that the ordinary skilled artisan would not be able to differentiate without further testing which peptides having 75% sequence identity to SEQ ID NO: 4 and inhibit an interaction between connexin-46 and c-Src from those peptides having 75% sequence identity and do not inhibit interactions between Cx46 and c-Src. Unless all peptides that comprise a sequence having at least 75% sequence identity to SEQ ID NO: 4 can modulate the activity of connexin-46, the disclosure of SEQ ID NO: 4 is not representative of the claimed sequence. Therefore, the specification fails to satisfy the written description requirement of 35 U.S.C. 112(a) or 35 U.S.C.112, first paragraph, with respect to claim 1-3, 5, 9, and 11.
Claims 2 and 8-12 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.
This is a new matter rejection.
Claim 2 recites that the TAT internalization sequence is operably linked to the connexin-46 mimetic domain. The specification of the instant invention states that the invention may include a TAT peptide sequence to facilitate the internalization of the mimetic peptide into the cell The specification submitted 28 March 2023 states that the sequence “may include” a TAT peptide sequence that facilitates internalization, but says nothing about how the TAT peptide sequence and SEQ ID NO: 4 are linked (pg. 7, “In a preferred embodiment, the mimetic peptide having between 75-100% amino acid sequence similarity to any of the amino acid sequences set forth in SEQ ID NO: 2, SEQ ID NO: 3 and SEQ ID NO: 4 may include a TAT peptide sequence (GRKKRRQRRR set forth in SEQ ID NO: 8) that facilitates the internalization of the mimetic peptide into the cell. The mimetic peptides, including said TAT peptide sequence, are shown in SEQ ID NO: 5, SEQ ID NO: 6 and SEQ ID NO: 7.”). The specification fails to disclose how the TAT peptide is strategically attached to the peptide (whether that is through a linker or a covalent bond). In the remarks filed 19 February, Applicant asserts that support for the amendments can be found “throughout the originally filed specification” (see pg. 6 of the remarks filed 19 February 2026), but fails to detail were in the specification support for the added limitation “wherein the peptide further comprises a TAT internalization sequence operably linked to the connexin-46 mimetic domain”, is located.
Claims 8-12 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, due to their dependency on claim 2, which is a rejected claim. Therefore, the specification also fails to disclose how the TAT peptide is “operably linked” to SEQ ID NO: 4, as necessitated by claims 8-12 due to their dependency from claim 2.
Claim Rejections - 35 USC § 112
Response to Arguments: The rejection of claims 5 and 6 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, for being indefinite, have been withdrawn in view of the amendments filed 19 February, 2026.
Claim Rejections - 35 USC § 102
Response to Arguments: Claims 1-6 were rejected under 35 U.S.C. 102(a)(2) as being anticipated by Bremel et al. (US 2013/0330335 A1), Venter et al. (US 6812339 B1), and de Goede et al. (HIV-1 evolution in patients undergoing immunotherapy with Tat, Rev, and Nef expressing dendritic cells followed by treatment interruption. AIDS 27(17):p 2679-2689, November 13, 2013). Applicants’ amendment, see page 4 of the response, filed 19 February 2026, with respect to claims 1-3 and 5, has been fully considered. The rejection of claims 1-3 and 5 has been withdrawn regarding SEQ ID NOs: 2, 3, and 5-7. Applicant’s amendments, see page 4, filed 19 February 2026, with respect to the cancellation of claims 4 and 6 have been fully considered. The rejection of claims 4 and 6 has been withdrawn.
Regarding claims 1 and 3, Applicant argues, that the cited references do not teach or suggest the inhibition of the interaction between connexin-46 and c-Src by peptides with at least 75% sequence identity to SEQ ID NO: 4, due to the claim reciting specific structural and functional limitations. See pages 8-9 of the response. The applicants’ arguments filed 19 February 2026 have been fully considered and were found unpersuasive.
In response to applicant's argument that the cited references do not teach or suggest the inhibition of the interaction between connexin-46 and c-Src and that structural similarity alone is insufficient to anticipate the claimed invention, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. With regard to the mimetic peptide inhibiting an interaction between connexin-46 and c-Src, the peptide of Venter et al. and Jarvis et al. comprise the amino acid sequence that is claimed to inhibit an interaction between connexin-46 and c-Src and because a chemical composition and its properties are inseparable, a person of ordinary skill in the art would reasonably expect the peptide of Venter et al. and Jarvis et al. to also inhibit an interaction between connexin-46 and c-Src .
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)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1 and 3 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Venter et al. (US 6812339 B1), in regard to SEQ ID NO: 4. This rejection is maintained.
Regarding claim 1, Venter et al. (US 6812339 B1) discloses peptide that has at least 75% amino acid similarity to the amino acid sequence as described PQMHQPPLP (SEQ ID NO: 4). See the peptide represented by SEQ ID NO: 7245; col. 6 lines. 10-16 “The sequence information provided in Table 1 includes … protein sequences (SEQ ID NOs: 5872-11,742) … for each human disease-associated gene that contains a SNP of the present invention”.
Regarding claim 3, with regard to the limitation “to be used in the treatment of cancer”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as described in Venter at al. contains the same structure as the peptide as described in SEQ ID NO: 4 of the instant claim, thus it is interpreted as being sufficient in the treatment of cancer as described in the instant claim.
Therefore, the disclosure of Jarvis et al. anticipates claims 1 and 3 of the presently claimed invention, and the rejection is maintained.
Claims 1 and 3 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)), in regard to SEQ ID NO: 4. This rejection is maintained.
Regarding claim 1, Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)) discloses a peptide that has at least 75% amino acid similarity to the amino acid sequence as described PQMHQPPLP (SEQ ID NO: 4). See the peptide represented by residues 88-96 of the Calcium Homeostasis Endoplasmic Reticulum Protein (CHERP) found in the genome of Chenopodium quinoa; page 307 “We sequenced and assembled the genome of the coastal Chilean quinoa accession PI 614886 (BioSample accession code SAMN04338310)”.
Regarding claim 3, with regard to the limitation “to be used in the treatment of cancer associated with overexpression of connexin-46”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as described in Jarvis et al. contains the same structure as the peptide as described in SEQ ID NO: 4 of the instant claim, thus it is interpreted as being sufficient in the treatment of cancer associated with overexpression of connexin-46 as described in the instant claim.
Therefore, the disclosure of Jarvis et al. anticipates claims 1 and 3 of the presently claimed invention, and the rejection is maintained.
Claims 1, 3 and 5 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Alsobrook et al. (US 2004/0067882 A1), in regard to SEQ ID NO: 4.
This rejection is new as necessitated by the amendment filed 19 February 2026.
Alsobrook et al. teaches three peptides (SEQ ID NOs: 32, 78, and 103) that all comprise sequences with at least 75% sequence similarity to the instant SEQ ID NO: 4. With regard to the mimetic peptide inhibiting an interaction between connexin-46 and c-Src, the peptides of Alsobrook et al. comprise the amino acid sequence that is claimed to inhibit an interaction between connexin-46 and c-Src and because a chemical composition and its properties are inseparable, a person of ordinary skill in the art would reasonably expect the peptide of Alsobrook et al. to also inhibit an interaction between connexin-46 and c-Src .
Regarding claim 3, with regard to the limitation “to be used in the treatment of cancer associated with overexpression of connexin-46”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptides as described in Alsobrook et al. contains the same structure as the peptide as described in SEQ ID NO: 4 of the instant claim, thus it is interpreted as being sufficient in the treatment of cancer associated with overexpression of connexin-46 as described in the instant claim.
Alsobrook also teaches the peptides as a part of a pharmaceutical composition and a pharmaceutically acceptable carrier and also teaching that pharmaceutical compositions of the peptides can contain physiological saline ([0012] “In another embodiment, the invention comprises a pharmaceutical composition involving a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 141 and a pharmaceutically acceptable carrier. ”; [0259] “Pharmaceutical compositions suitable for injectable use include sterile aqueous solutions (where water soluble) or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersion. For intravenous administration, suitable carriers include physiological saline…”).
Claim Rejections - 35 USC § 103
Response to Arguments: Claims 1 and 2 were rejected under 35 U.S.C. 103 as being unpatentable over Bremel et al. (US 2013/0330335 A1), Venter et al. (US 6812339 B1), and de Goede et al. (HIV-1 evolution in patients undergoing immunotherapy with Tat, Rev, and Nef expressing dendritic cells followed by treatment interruption. AIDS 27(17):p 2679-2689, November 13, 2013), in view of Bonny (US 2002/0127676 A1). Applicants’ amendment, see page 4 of the response, filed 19 February 2026, with respect to claims 1 and 2, has been fully considered. The rejection of claims 1 and 2 has been withdrawn regarding SEQ ID NOs: 2, 3, and 5-7.
Applicants argue, that Venter et al. does not teach or suggest the inhibition of the interaction between connexin-46 and c-Src by peptides with at least 75% sequence identity to SEQ ID NO: 4, due to the claim reciting specific structural and functional limitations. See pages 9-10 of the response. The applicants’ arguments filed 19 February 2026 have been fully considered and were found unpersuasive.
In response to applicant's argument that the cited references do not disclose or suggest elements of the claims, “including (i) a defined relationship to SEQ ID NO: 4 or SEQ ID NO: 7, (ii) inhibition of the interaction between connexin-46 and c-Src, and (iii) therapeutic use limited to cancers associated with overexpression of connexin-46.”. If the prior art structure is capable of performing the intended use, then it meets the claim. With regard to a defined relationship, inhibition of interactions and/or therapeutic uses, the peptide of Venter et al. comprises the amino acid sequence that is claimed to modulate connexin-46 and inhibit an interaction between connexin-46 and c-Src, and because a chemical composition and its properties are inseparable, a person of ordinary skill in the art would reasonably expect the peptide of Venter et al. to also modulate connexin-46. MPEP 2112.01 (II).
Applicants argue, that Jarvis et al. does not teach or suggest the inhibition of the interaction between connexin-46 and c-Src by peptides with at least 75% sequence identity to SEQ ID NO: 4, due to the claim reciting specific structural and functional limitations. See pages 9-10 of the response. The applicants’ arguments filed 19 February 2026 have been fully considered and were found unpersuasive.
In response to applicant's argument that the cited references do not disclose or suggest elements of the claims, “including (i) a defined relationship to SEQ ID NO: 4 or SEQ ID NO: 7, (ii) inhibition of the interaction between connexin-46 and c-Src, and (iii) therapeutic use limited to cancers associated with overexpression of connexin-46.”. If the prior art structure is capable of performing the intended use, then it meets the claim. With regard to a defined relationship, inhibition of interactions and/or therapeutic uses, the peptide of Jarvis et al. comprises the amino acid sequence that is claimed to modulate connexin-46 and inhibit an interaction between connexin-46 and c-Src, and because a chemical composition and its properties are inseparable, a person of ordinary skill in the art would reasonably expect the peptide of Jarvis et al. to also modulate connexin-46. MPEP 2112.01 (II).
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 2 is rejected under 35 U.S.C. 103 as being unpatentable over Venter et al. (US 6812339 B1), as applied to claim 1, in view of Bonny (US 2002/0127676 A1), in regard to SEQ ID NO: 4. This rejection is maintained.
Regarding claim 2, Venter et al. (US 6812339 B1) discloses peptide that has at least 75% amino acid similarity to the amino acid sequence as described PQMHQPPLP (SEQ ID NO: 4). See the peptide represented by SEQ ID NO: 7245; col. 6 lines. 10-16 “The sequence information provided in Table 1 includes … protein sequences (SEQ ID NOs: 5872-11,742) … for each human disease-associated gene that contains a SNP of the present invention”.
Venter et al. does not teach SEQ ID NO: 4 with a TAT internalization sequence operably linked to the connexin-46 mimetic domain.
Bonny teaches a teaches the TAT protein described in the instant claims and its ability to facilitate the internalization of a peptide; ([0061] “A trafficking sequence is any sequence of amino acids that directs a peptide in which it is present to a desired cellular destination … can direct the peptide across the plasma membrane, e.g., from outside the cell, through the plasma membrane, and into the cytoplasm; [0062] the trafficking peptide is derived from a known membrane-translocating sequence … fragment includes a peptide containing TAT residues 48-57, e.g. NH2-GRKKRRQRRR-COOH [SEQ ID NO: 7] … A TAT peptide that includes the region that mediates entry and uptake into cells can be further defined using known techniques.”)
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Venter et al.’s taught peptides by combining them with the HIV TAT peptide taught by Bonny in order to increase peptide internalization. This modification of the art takes a known peptide and known method used to mediate the entry and uptake of a peptide.
One would have had a reasonable expectation of success because the well-established function of HIV TAT as a cell penetrating peptide is used in the art to facilitate intracellular transport of cells under KSR rationale D. (See MPEP 2143 (I)(D)).
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)), as applied to claim 1, in view of Bonny (US 2002/0127676 A1), in regard to SEQ ID NO: 4. This rejection is maintained.
Regarding claim 2, Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)) discloses a peptide that has at least 75% amino acid similarity to the amino acid sequence as described PQMHQPPLP (SEQ ID NO: 4). See the peptide represented by residues 88-96 of the Calcium Homeostasis Endoplasmic Reticulum Protein (CHERP) found in the genome of Chenopodium quinoa; page 307 “We sequenced and assembled the genome of the coastal Chilean quinoa accession PI 614886 (BioSample accession code SAMN04338310)”.
Jarvis et al. does not teach SEQ ID NO: 4 with a TAT internalization sequence operably linked to the connexin-46 mimetic domain.
Bonny teaches a teaches the TAT protein described in the instant claims and its ability to facilitate the internalization of a peptide; ([0061] “A trafficking sequence is any sequence of amino acids that directs a peptide in which it is present to a desired cellular destination … can direct the peptide across the plasma membrane, e.g., from outside the cell, through the plasma membrane, and into the cytoplasm; [0062] the trafficking peptide is derived from a known membrane-translocating sequence … fragment includes a peptide containing TAT residues 48-57, e.g. NH2-GRKKRRQRRR-COOH [SEQ ID NO: 7] … A TAT peptide that includes the region that mediates entry and uptake into cells can be further defined using known techniques.”)
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Jarvis et al.’s taught peptides by combining them with the HIV TAT peptide taught by Bonny in order to increase peptide internalization. This modification of the art takes a known peptide and known method used to mediate the entry and uptake of a peptide.
One would have had a reasonable expectation of success because the well-established function of HIV TAT as a cell penetrating peptide is used in the art to facilitate intracellular transport of cells under KSR rationale D. (See MPEP 2143 (I)(D)).
Claims 2, 9 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Alsobrook et al. (US 2004/0067882 A1), as applied to claim 1, in view of Bonny (US 2002/0127676 A1), in regard to SEQ ID NO: 4.
This rejection is new as necessitated by the amendment filed 19 February 2026.
Regarding claim 2, Alsobrook et al. teaches three peptides (SEQ ID NOs: 32, 78, and 103) that all comprise sequences with at least 75% sequence similarity to the instant SEQ ID NO: 4. With regard to the mimetic peptide inhibiting an interaction between connexin-46 and c-Src, the peptides of Alsobrook et al. comprise the amino acid sequence that is claimed to inhibit an interaction between connexin-46 and c-Src and because a chemical composition and its properties are inseparable, a person of ordinary skill in the art would reasonably expect the peptide of Alsobrook et al. to also inhibit an interaction between connexin-46 and c-Src .
Alsobrook et al. does not teach SEQ ID NO: 4 with a TAT internalization sequence operably linked to the connexin-46 mimetic domain.
Bonny teaches a teaches the TAT protein described in the instant claims and its ability to facilitate the internalization of a peptide; ([0061] “A trafficking sequence is any sequence of amino acids that directs a peptide in which it is present to a desired cellular destination … can direct the peptide across the plasma membrane, e.g., from outside the cell, through the plasma membrane, and into the cytoplasm; [0062] the trafficking peptide is derived from a known membrane-translocating sequence … fragment includes a peptide containing TAT residues 48-57, e.g. NH2-GRKKRRQRRR-COOH [SEQ ID NO: 7] … A TAT peptide that includes the region that mediates entry and uptake into cells can be further defined using known techniques.”)
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Alsobrook et al.’s taught peptides by combining them with the HIV TAT peptide taught by Bonny in order to increase peptide internalization. This modification of the art takes a known peptide and known method used to mediate the entry and uptake of a peptide.
One would have had a reasonable expectation of success because the well-established function of HIV TAT as a cell penetrating peptide is used in the art to facilitate intracellular transport of cells under KSR rationale D. (See MPEP 2143 (I)(D)).
Regarding claim 9, in regard to the limitation “for the treatment of cancer associated with overexpression of connexin-46”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as realized by the combination of Alsobrook at al. and Bonny contains the necessary components of the claims from which claim 9 depends, thus it is interpreted as being sufficient in the treatment of cancer associated with overexpression of connexin-46, as described in the instant claim.
Regarding claim 11, Alsobrook teaches three peptides (SEQ ID NOs: 32, 78, and 103) that all comprise sequences with at least 75% sequence similarity to the instant SEQ ID NO: 4 and the peptide being in a pharmaceutical composition comprising the peptide and a pharmaceutically acceptable excipient ([0012] “In another embodiment, the invention comprises a pharmaceutical composition involving a polypeptide with an amino acid sequence selected from the group consisting of SEQ ID NO: 2n, wherein n is an integer between 1 and 141 and a pharmaceutically acceptable carrier. ”; [0259] “Pharmaceutical compositions suitable for injectable use include sterile aqueous solutions (where water soluble) or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersion. For intravenous administration, suitable carriers include physiological saline…”).
In regard to the limitation “wherein the mimetic peptide inhibits an interaction between connexin-46 and c-Src.” (from claim 1), a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as realized by the combination of Alsobrook at al. and Bonny contains the necessary components of the claims from which claim depends, thus it is interpreted as being sufficient in inhibiting an interaction between connexin-46 and c-Src, as described in claim 1.
Claim 9 is rejected under rejected under 35 U.S.C. 103 as being unpatentable over Venter et al. (US 6812339 B1), as applied to claim 1, in view of Bonny (US 2002/0127676 A1).
The rejection below is new as necessitated by the amendment filed 19 February 2026.
Regarding claim 9, Venter et al. teaches a peptide (SEQ ID NO: 7245) that comprises a sequence with at least 75% sequence similarity to the instant SEQ ID NO: 4, as required by claim 1.
Venter et al. does not teach SEQ ID NO: 4 with a TAT internalization sequence operably linked to the connexin-46 mimetic domain.
Bonny teaches a teaches the TAT protein described in the instant claims and its ability to facilitate the internalization of a peptide; ([0061] “A trafficking sequence is any sequence of amino acids that directs a peptide in which it is present to a desired cellular destination … can direct the peptide across the plasma membrane, e.g., from outside the cell, through the plasma membrane, and into the cytoplasm; [0062] the trafficking peptide is derived from a known membrane-translocating sequence … fragment includes a peptide containing TAT residues 48-57, e.g. NH2-GRKKRRQRRR-COOH [SEQ ID NO: 7] … A TAT peptide that includes the region that mediates entry and uptake into cells can be further defined using known techniques.”)
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Venter et al.’s taught peptides by combining them with the HIV TAT peptide taught by Bonny in order to increase peptide internalization. This modification of the art takes a known peptide and known method used to mediate the entry and uptake of a peptide.
One would have had a reasonable expectation of success because the well-established function of HIV TAT as a cell penetrating peptide is used in the art to facilitate intracellular transport of cells under KSR rationale D. (See MPEP 2143 (I)(D)).
In regard to the limitation “for the treatment of cancer associated with overexpression of connexin-46”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as realized by the combination of Venter at al. and Bonny contains the necessary components of the claims from which claim 9 depends, thus it is interpreted as being sufficient in the treatment of cancer associated with overexpression of connexin-46, as described in the instant claim.
Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)), as applied to claim 1, in view of Bonny (US 2002/0127676 A1), in regard to SEQ ID NO: 4. This rejection is maintained.
Regarding claim 9, Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)) discloses a peptide that has at least 75% amino acid similarity to the amino acid sequence as described PQMHQPPLP (SEQ ID NO: 4). See the peptide represented by residues 88-96 of the Calcium Homeostasis Endoplasmic Reticulum Protein (CHERP) found in the genome of Chenopodium quinoa; page 307 “We sequenced and assembled the genome of the coastal Chilean quinoa accession PI 614886 (BioSample accession code SAMN04338310)”.
Jarvis et al. does not teach SEQ ID NO: 4 with a TAT internalization sequence operably linked to the connexin-46 mimetic domain.
Bonny teaches a teaches the TAT protein described in the instant claims and its ability to facilitate the internalization of a peptide; ([0061] “A trafficking sequence is any sequence of amino acids that directs a peptide in which it is present to a desired cellular destination … can direct the peptide across the plasma membrane, e.g., from outside the cell, through the plasma membrane, and into the cytoplasm; [0062] the trafficking peptide is derived from a known membrane-translocating sequence … fragment includes a peptide containing TAT residues 48-57, e.g. NH2-GRKKRRQRRR-COOH [SEQ ID NO: 7] … A TAT peptide that includes the region that mediates entry and uptake into cells can be further defined using known techniques.”)
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify Jarvis et al.’s taught peptides by combining them with the HIV TAT peptide taught by Bonny in order to increase peptide internalization. This modification of the art takes a known peptide and known method used to mediate the entry and uptake of a peptide.
One would have had a reasonable expectation of success because the well-established function of HIV TAT as a cell penetrating peptide is used in the art to facilitate intracellular transport of cells under KSR rationale D. (See MPEP 2143 (I)(D)).
In regard to the limitation “for the treatment of cancer associated with overexpression of connexin-46”, a recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim. The peptide as realized by the combination of Jarvis at al. and Bonny contains the necessary components of the claims from which claim 9 depends, thus it is interpreted as being sufficient in the treatment of cancer associated with overexpression of connexin-46, as described in the instant claim.
Allowable Subject Matter
The following is a statement of reasons for the indication of allowable subject matter: SEQ ID NOs: 4 and 7, as recited in claims 1-3, 5 and 8-12, were not taught in the prior art in a 100% embodiment. The closest sequence match is a segment of the nucleotide sequence described in Jarvis et al. (The genome of Chenopodium quinoa. Nature 542, 307–312 (2017)) with 92.7% sequence similarity to the instant SEQ ID NO: 4, as seen below. The closest sequence match is a segment of the nucleotide sequence described in de Goede et al. (HIV-1 evolution in patients undergoing immunotherapy with Tat, Rev, and Nef expressing dendritic cells followed by treatment interruption. AIDS 27(17):p 2679-2689, November 13, 2013) with 76.4% sequence similarity to the instant SEQ ID NO: 7, as seen below.
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Claims 8, 10 and 12 are objected to as being dependent upon a rejected base claim (claim 2), but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Claims 8, 10 and 12 contain allowable subject matter. Claim 8 is drawn to a mimetic peptide comprising the amino acid sequence of SEQ ID NO: 7. For the sake of compact prosecution, the Examiner is interpreting the claim to mean SEQ ID NO: 7 in a 100% embodiment. The closest sequence match is a segment of the nucleotide sequence described in de Goede et al. (HIV-1 evolution in patients undergoing immunotherapy with Tat, Rev, and Nef expressing dendritic cells followed by treatment interruption. AIDS 27(17):p 2679-2689, November 13, 2013) with 76.4% sequence similarity to the instant SEQ ID NO: 7, as seen above.
Summary
Claims 1-3, 5, and 8-12 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph. Claims 1, 3, and 5 are rejected under 35 U.S.C. 102(a)(2). Claims 2, 9, and 11 are rejected under 35 U.S.C. 103. Claims 8, 10 and 12 are objected.
No claims are allowed.
Conclusion
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.
/Daliyah M. Brown/Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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