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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 7/17/2026 has been entered.
Election/Restrictions
Applicant’s election without traverse of Group I, (A) pheophorbide-a, (B) SEQ ID NO:1, (C) LXY30
in the reply filed on 7/14/2025 is acknowledged.
Claim 7, 15-23, 26-27, 29-33, 35, 60-61, 64 withdrawn from further consideration pursuant to 37
CFR 1.142(b) as being drawn to a nonelected Group II-V and species of A, B, and C, there being no
allowable generic or linking claim. Election was made without traverse in the reply filed on 7/14/2025.
Status of Claims
Cancelled: 13, 15, 17, 18, 34, 36-59, 62, 63
Withdrawn: 7, 16, 19-23, 26, 27, 29-33, 35, 60-61, 64
Examined Herein: 1-6, 8-12, 14, 24, 25, 28
Priority
Acknowledgment is made of applicant's claim for priority under based upon an application filed
in PRO 62/886,698 on 8/14/2019, PRO 62/886,718 on 8/14/2019, and PCT/US20/46495 on 8/14/2020.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 11/2/2022, 7/14/2025, and 2/18/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is
being considered by the examiner.
Drawings
The drawings received on 2/10/2022 are accepted.
Withdrawn Rejections
The rejection of claims 1-8, 11, 12, and 24 under 35 U.S.C. 103 over Choi and Hamblett is hereby withdrawn in view of Applicant’s amendments to claim 1 and persuasive arguments that Choi and Hamblett do not teach the claimed limitations, as amended.
The rejection of claims 1-4, 9-14, 24, 25, and 28 under 35 U.S.C. 103 over Xu and Xiao is hereby withdrawn in view of Applicant’s amendments to claim 1 and persuasive arguments that Xu and Xiao do not teach the claimed limitations, as amended.
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.
Claims 1-4, 9-12, and 14 are rejected under 35 U.S.C. 103 as being unpatentable over Xu (Bio-inspired metal ions regulate the structure evolution of self-assembled peptide-based nanoparticles, 6/22/2016, Nanoscale, 8:14078-14083), in view of Lam (US 2013/0172270 A1, Published 7/4/2013).
With respect to claim 1, Xu discloses a compound of formula (I), BP-KLVFFK-RGD:
A-B-C (I)
wherein:
A is a hydrophobic moiety, bis-pyrene,
B is a peptide, KLVFFK, that forms a beta-sheet and comprises sequence identity SEO ID NO: 1;
C is a hydrophilic targeting ligand, RGD. [Xu, Page 14079, Scheme 1 and Figure 1]
With respect to claims 2-4, Xu discloses that the hydrophobic moiety is bis-pyrene. [Xu, Page 14079, Scheme 1 and Figure 1] Bis-pyrene is a fluorescent dye.
With respect to claims 9-10, Xu discloses that the peptide, KLVFFK, is a sequence of 6 amino acids in length. [Xu, Page 4087, Figure 1(a) and Col. 1, Paragraph 2 – Col. 2, Paragraph 1]
With respect to claims 11-12, Xu discloses that the peptide is KLVFFK. [Xu, Page 14079, Scheme 1 and Figure 1] KLVFFK comprises a peptide sequence, KLVFF, from a beta-sheet peptide domain of beta-amyloid 40.
With respect to claim 14, Xu discloses that the peptide is KLVFFK. [Xu, Page 14079, Scheme 1 and Figure 1] KLVFFK comprises SEQ ID: NO 1.
Xu further discloses that RGD binds to αvβ3 integrin on U87 and MCF-7 cells. [Xu, Page 14078, Col. 2, Paragraph 2]
Xu does not disclose that the hydrophilic targeting ligand is a LLP2A prodrug, LLP2A, LXY30, LXW64, DUPA, folate, a LHRH peptide, or a toll-like receptor agonist CpG oligonucleotide.
However, with respect to claim 1, Lam discloses several RGD peptides of formula (I), including LXW64, that target αvβ3 integrin on tumor cells. [Lam, 0006, 0019] Lam further discloses there is a need for better and different binding agents of αvβ3 integrin that can have improved targeting efficacy, lower nonspecific binding to normal organs, and carry payloads of therapeutics and/or diagnostics. To that end, Lam discloses LXW64 satisfies this and other needs. [Lam, 0005]
Modifying the compound disclosed by Xu by replacing RGD with LXW64 results in the compound of claim 1, wherein the hydrophilic targeting ligand is LXW64.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Xu by replacing RGD with LXW64 and have a reasonable expectation of success. Xu discloses a conjugate BP-KLVFF-RGD comprising a targeting ligand, RGD, that binds to αvβ3 integrin on U87 and MCF-7 cells. Lam discloses several RGD peptides, including LXW64, that target αvβ3 integrin on tumor cells. Accordingly, the combined teachings of Xu and Lam reasonably suggest that LXW64 may function as the RGD peptide in the conjugate disclosed by Xu, as it also binds to αvβ3 integrin on tumor cells. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II). In the present case, Lam discloses that, compared with commonly used RGD ligands, LXW64 has improved targeting efficacy and lower nonspecific binding to normal organs, and can be functionalized to conjugate an imaging payload without decreasing binding strength. [Lam, 0019] Therefore, one would have been motivated by the expectation that replacing RGD with LXW64 would enable the conjugate disclosed by Xu to exhibit improved targeting efficacy, lower nonspecific binding to normal organs, and be functionalized to conjugate an imaging payload without decreasing binding strength.
Claims 1-4, 9-12, 14 and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Castillo (US 2011/0207662 A1, Published 8/25/2011).
With respect to claim 1, Castillo discloses a compound of the following formula:
Binding moiety—Cleavable moiety—Peptide
[0056]
wherein:
The binding moiety is a hydrophobic group. In a specific embodiment, the hydrophobic moiety is an alkyl group (e.g., an alkyl group of 6 to 36 carbon units), cholesterol, or fluorescein; [0081, 0098]
The cleavable moiety links the biologically active peptide and the binding moiety. In a specific embodiment, the cleavable moiety is His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys (SEQ ID NO: 15) or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu (SEQ ID NO: 17); [0092]
The peptide is a biologically active polyamino acid ranging from 5 to 100 amino acids. In a specific embodiment, the peptide is EGF, EGFR, TGF-α, gonadotropin releasing hormone (GnRH), or LHRH. [0060]
Accordingly, in one embodiment, Castillo discloses a compound of formula (I):
A-B-C (I)
wherein:
A is a hydrophobic moiety including an alkyl group (e.g., an alkyl group of 6 to 36 carbon units), cholesterol or fluorescein;
B is a peptide, His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu, wherein the peptide forms a beta-sheet and comprises (i) SEO ID NO: 1;
C is a hydrophilic targeting ligand including a LHRH peptide or an EGFR ligand.
With respect to claim 2, Castillo discloses the hydrophobic moiety is a dye (fluorescein). [0098]
With respect to claims 3 and 4, Castillo discloses the hydrophobic moiety is a fluorescent dye or cholesterol. [0098]
With respect to claims 9 and 10, Castillo discloses the peptide is a peptide sequence 9 or 12 amino acids in length. [0092]
With respect to claims 11 and 12, Castillo discloses the peptide comprises KLVFF. [0092] KLVFF is a peptide sequence from a beta-sheet peptide domain of beta-amyloid 40.
With respect to claim 14, Castillo discloses the peptide comprises SEQ ID NO: 1. [0092]
With respect to claim 24, Castillo discloses the hydrophilic targeting ligand is an LHRH peptide, or an EGFR ligand. [0060]
Modifying the compound disclosed by Castillo by selecting cholesterol or fluorescein as the binding/hydrophobic moiety, His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu as the cleavable moiety/peptide, and EGF, EGFR, TGF-α, GnRH, or LHRH as the biologically active peptide/hydrophilic ligand results in the compound of claim 1.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by selecting cholesterol or fluorescein as the binding/hydrophobic moiety, His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu as the cleavable moiety/peptide, and EGF, EGFR, TGF-α, GnRH, or LHRH as the biologically active peptide/hydrophilic ligand and have a reasonable expectation of success. Castillo discloses a compound of the following formula: binding moiety—cleavable moiety—peptide, wherein in a specific embodiment, the hydrophobic moiety may be an alkyl group, cholesterol or fluorescein, the cleavable moiety may be His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu and the biologically active peptide may be EGF, EGFR, TGF-α, GnRH or LHRH. In view of this express teaching by Castillo, it is reasonable to expect that the disclosed compound may be modified by selecting the expressly taught embodiments of each of the binding/hydrophobic moiety, the cleavable moiety/peptide, and the biologically active peptide/hydrophilic ligand. One would have been motivated to do so because the selection of a known material based on its suitability for its intended use is prima facie obvious. MPEP 2144.07. In the present case, the selection of cholesterol or fluorescein, His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu, and EGF, EGFR, TGF-α, GnRH, or LHRH based on their suitability to function as the binding/hydrophobic moiety, the cleavable moiety/peptide, and/or the biologically active peptide/hydrophilic ligand in the compound disclosed by Castillo is prima facie obvious.
Claims 1-4, 9-12, 14, 24, 25, and 28 are rejected under 35 U.S.C. 103 as being unpatentable over Castillo, as applied to claims 1-4, 9-12, 14, and 24 above, and further in view of Xiao (WO 2017/031084 A1, Published 2/23/2017).
With respect to claim 1, Castillo discloses the teachings above.
With respect to claims 1, 24, 25, and 28, Castillo discloses that the biologically active peptide refers to a peptide that binds to a cellular receptor. [Castillo, 0059] In a specific embodiment, the biologically active peptide is GM-CSF, G-CSF, blood clotting factor VII, blood clotting factor VIII, or LHRH. [Castillo, 0060]
Castillo does not disclose that the hydrophilic targeting ligand is an LLP2A prodrug, LLP2A, LXY30, LXW64, DUPA, folate, a HER2 ligand, or a toll-like receptor agonist CpG oligonucleotide.
However, with respect to claims 1, 24, 25, and 28, Xiao discloses that LHRH, coagulation factors, G-CSF, GM-CSF, folic acid, LLP2A, and LXY30 are each a cellular targeting moiety. [Xiao, 0095, 0178]
Modifying the compound disclosed by Castillo by replacing the biologically active peptide with LLP2A or LXY30 results in the compound of claim 1, 24, 25, and/or 28.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Castillo by replacing the biologically active peptide with LLP2A or LXY30 and have a reasonable expectation of success. Castillo discloses a compound comprising the following formula: binding moiety—cleavable moiety— biologically active peptide; wherein the biologically active peptide is a peptide that binds to a cellular receptor including GM-CSF, G-CSF, blood clotting factor VII, blood clotting factor VIII, or LHRH. Xiao discloses that LHRH, G-CSF, GM-CSF, coagulation factors, and additionally LLP2A and LXY30 are cellular targeting moieties. The combined teachings of Castillo and Xiao reasonably suggest that the biologically active peptide may alternatively be LLP2A and LXY30, as they are also peptides that bind to a cellular receptor. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II). In the present case, LLP2A and LXY30 can bind to targets other than GM-CSF, G-CSF, blood clotting factor VII, blood clotting factor VIII, and LHRH, and localize to a particular tumor, tissue, organ, or other region of the body. [Xiao, 0095, 0176, 0177] For example, Xiao discloses that LLP2A is specific for α4β1 integrin. [Xiao, 0095] Therefore, one would have been motivated by the expectation that replacing the biologically active peptide would enable the compound to bind to a desired target and localize in a desired region of the body.
Claims 1-6, 8-12, 14, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Castillo, as applied to claims 1-4, 9-12, 14, and 24 above, and further in view of Li (US 2014/0161719 A1, Published 6/12/2014).
With respect to claim 1, Castillo discloses the teachings above.
With respect to claims 3-6, 8, Castillo discloses that the binding moiety is alternatively a metal-binding (or chelating) group capable of forming a complex between the metal ion and the chemical groups by coordinate bonds. [Castillo, 0082-0084]
Castillo does not disclose that the binding/hydrophobic moiety is porphyrin.
However, with respect to claims 3-6, 8, Li discloses that porphyrins, specifically pyropheophorbide-a, pheophorbide, chlorin e6, purpurin, and purpurinimide, can be chelated to a metal. [Li, 0059, 0094]
Modifying the compound disclosed by Castillo by replacing the binding/hydrophobic moiety with a porphyrin selected from pyropheophorbide-a, pheophorbide, chlorin e6, purpurin, and/or purpurinimide results in the compound of claim 3, 4, 5, 6, and/or 8.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Castillo by replacing the binding/hydrophobic moiety with a porphyrin selected from pyropheophorbide-a, pheophorbide, chlorin e6, purpurin, and/or purpurinimide and have a reasonable expectation of success. Castillo discloses a compound comprising the following formula: binding moiety—cleavable moiety— biologically active peptide; wherein the binding moiety is a metal-binding (or chelating) group that is capable of forming a complex between the metal ion and the chemical groups by coordinate bonds. Li discloses that porphyrins, in pyropheophorbide-a, pheophorbide, chlorin e6, purpurin, and purpurinimide can be chelated to a metal. Accordingly, the combined teachings of Castillo and Li suggest that pyropheophorbide-a, pheophorbide, chlorin e6, purpurin, and purpurinimide may function as the binding (or chelating) group in the compound disclosed by Castillo. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II). In the present case, metal-binding groups, including porphyrins, can bind various moieties, including metal chelate ions. [Castillo, 0085][Li, 0161] Therefore, one would have been motivated by the expectation that replacing the binding/hydrophobic moiety with a porphyrin would enable the compound to exhibit the additional capability of binding various moieties, including metal chelate ions.
Claims 1-4, 9-12, 14, 24, 25, and 28 are rejected under 35 U.S.C. 103 as being unpatentable over
Wang (WO 2017/156427 A1, Published 9/14/2017), in view of Castillo and Lac (US 2018/0140715 A1, Published 5/24/2018).
With respect to claim 1, a compound of the following formula:
Peptide Ligand - R2 or Peptide Ligand-L-A
[Wang, 0006]
wherein:
The peptide ligand is a compound of Formula (I) and increases the attachment of endothelial cells and/or endothelial progenitor cells to the scaffold. [Wang, 0006, 0094] In a specific embodiment, the peptide is LXW7. [Wang, 0094] The peptide ligand can have an affinity for a cell surface integrin and bind one or more of integrins α4β1, α5β1, α6β1, ανβ3 and ανβ5. In some embodiments, the peptide ligand binds to integrin ανβ3 on the cells; [Wang, 0095]
L is a linker possessing one or more different reactive functional groups that allow for covalent attachment of moieties. [Wang, 0083] The linkers can be cleavable linkers designed for cleavage in the presence of particular conditions or in a particular environment. The cleavable linkers can be sensitive to, for example, protease activity; [Wang, 0084]
A is an active agent including biotin, drugs, radiolabels, imaging agents (i.e., fluorescein, Cy2, Cy3, Cy5 or Cy5.5), chemotherapy agents and nanoparticles. [Wang, 0085, 0086]
Accordingly, in one embodiment, Wang discloses a compound of formula (I):
A-B-C (I)
wherein:
A is a hydrophobic moiety including biotin or fluorescein; and
C is a hydrophilic targeting ligand LXW7.
With respect to claim 2, Wang discloses that the hydrophobic moiety is a dye including fluorescein, Cy2, Cy3, Cy5 or Cy5.5. [Wang, 0085]
With respect to claim 3, Wang discloses that the hydrophobic moiety is a fluorescent dye including fluorescein, Cy2, Cy3, Cy5 or Cy5.5. [Wang, 0085, 0086]
With respect to claim 4, Wang discloses that the hydrophobic moiety is a cyanine dye including Cy2, Cy3, Cy5 or Cy5.5. [Wang, 0085, 0086]
Wang does not disclose that B is a peptide, wherein the peptide forms a beta-sheet and comprises SEQ ID NO: 1, 2, or 3, or the hydrophilic targeting ligand is a LLP2A prodrug, LLP2A, LXY30, LXW64, DUPA, folate, a LHRH peptide, a HER2 ligand, an EGFR ligand, or a toll-like receptor agonist CpG oligonucleotide.
However, with respect to claim 1, Castillo discloses cleavable moieties that serve as linkers between a biologically active peptide and a binding moiety and include an amino acid sequence that can serve as a substrate for a protease. In a specific embodiment, the linkers include His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys (SEQ ID NO: 15) and Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu (SEQ ID NO: 17). [Castillo, 0092]
Furthermore, Lac discloses that LXY30 is an α3β1-integrin ligand and LLP2A is a peptidomimetic that can to bind to α4β1 integrin. [Lac, 0043, 0119]
Modifying the compound disclosed by Wang by replacing the linker with His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu and by replacing the peptide/hydrophobic targeting ligand with LXY30 or LLP2A results in the compound of claim 1, wherein:
A is a hydrophobic moiety including biotin or fluorescein;
B is a peptide, His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu, that forms a beta-sheet and comprises (i) SEO ID NO: 1; and
C is a hydrophilic targeting ligand LXY30 or LLP2A.
In which case, with respect to claims 9 and 10, Wang, Castillo, and Lac disclose that the peptide is a peptide sequence 9 or 12 amino acids in length.
With respect to claims 11 and 12, Wang, Castillo, and Lac disclose that the peptide comprises KLVFF. KLVFF is a peptide sequence from a beta-sheet peptide domain of beta-amyloid 40.
With respect to claim 14, Wang, Castillo, and Lac disclose that the peptide comprises SEQ ID NO: 1.
With respect to claim 24 and 25, Wang, Castillo, and Lac disclose that the hydrophilic targeting ligand is LLP2A or LXY30.
With respect to claim 24 and 28, Wang, Castillo, and Lac disclose that the hydrophilic targeting ligand is LXY30.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Wang by replacing the peptide/hydrophobic targeting ligand with LXY30 or LLP2A and have a reasonable expectation of success. Wang discloses a compound of the following formula: peptide Ligand-L-A; wherein the peptide ligand (Formula I) is derived from cRGD and increases the attachment of endothelial cells and/or endothelial progenitor cells to the scaffold. In a specific embodiment, the peptide is LXW7 or a peptide ligand that has an affinity for a cell surface integrin and/or binds one or more of the integrins α4β1, α5β1, α6β1, ανβ3 and ανβ5. Lac discloses that LXY30 binds to an α3β1-integrin ligand and LLP2A binds to α4β1 integrin. The combined teachings of Wang and Lac reasonably suggest that LXY30 or LLP2A may function as the peptide ligand in the compound disclosed by Wang, because both LXY30 and LLP2A have affinity for a cell-surface integrin. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II). In the present case, Lac discloses an antibody conjugate for cross-linking activated T cells to target cancer cells containing α3β1-integrin ligand LXY30 as an active agent. Binding of the antibody to the T cell and the ligand to a target cancer cell expressing α3β1-integrin delivers an activated T cell to the target cancer cell, enhancing anti-tumor efficacy. [Lac, 0043] Lac further discloses an antibody conjugate containing LLP2A. The conjugate was able to bind to α4β1 integrin on cancerous Jurkat cells. [Lac, 0119] Therefore, one would have been motivated by the expectation that replacing LXW7 with LXY30 could enable the conjugate disclosed by Wang to enhance anti-tumor efficacy by targeting an efficacious agent to a target cancer cell that expresses α3β1-integrin. One would have been motivated by the expectation that replacing LXW7 with LLP2A could enable the conjugate disclosed by Wang to be utilized to facilitate delivery of cargo to tumor sites for immunotherapy.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Wang by replacing the linker with His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu and have a reasonable expectation of success. Wang discloses a compound of the following formula: peptide Ligand-L-A; wherein L is a linker possessing one or more different reactive functional groups that allow for covalent attachment of moieties. The linkers can be cleavable and designed to cleave under particular conditions or in a particular environment. Castillo discloses cleavable moieties that serve as linkers between a biologically active peptide and a binding moiety, including His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys and Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu. The combined teachings of Wang and Castillo suggest that His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu may serve as the linker in the compound disclosed by Wang, as both linkers possess reactive functional groups that allow for covalent attachment of moieties and can be cleaved in the presence of particular conditions or in a particular environment. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II). In the present case, Castillo discloses that the cleavable moiety is useful when the binding moiety interferes with the biological activity of peptides. [Castillo, 0056] Therefore, one would have been motivated by the expectation that replacing the linker in the compound disclosed by Wang with His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Lys or Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu would be useful for the compound when the binding moiety (or hydrophobic moiety represented by “A” interferes with the biological activity of the peptide ligand.
Response to Arguments
Applicant’s arguments, filed 7/17/2026, with respect to the rejection of the pending claims under 35 U.S.C. 103 have been fully considered and are persuasive. Applicant’s arguments essentially state that the cited references do not teach the instant claim limitations, as amended. [Remarks 7/17/2026, Page 10, Paragraph 3; Page 11, Paragraph 3] Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground of rejection is made in view of the references cited above.
Applicant asserts, “Applicant respectfully requests rejoinder of the above withdrawn claims, pursuant to MPEP § 821.04(b)…. Note that, in this application, withdrawn claims 7, 16, 19 to 23, 26, 27, 29 to 33, 35, 60, 61, and 64 require all the limitations of product claim 1 and thus meet the requirement as set forth in the above-recited MPEP provision.” [Remarks 7/17/2026, Page 9 and 10, “I. REQUEST FOR REJOINDER”]
Applicant’s request for rejoinder under MPEP § 821.04(b) is noted but premature, as no product claim has been found allowable. However, the Office will follow proper procedure for rejoinder once a product claim is found allowable.
Conclusion
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/K.A.C./Examiner, Art Unit 1618
/Michael G. Hartley/Supervisory Patent Examiner, Art Unit 1618
