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 .
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.
Status of Claims
Claims 52-71 are pending and under examination.
Claim Objections
Claims 55-56 and 65 are objected to because of the following informalities:
Claims 55 and 56 recite “5 amino acids residues” should be – 5 amino acid residues –.
Claim 65 recites abbreviated terms that require the unabbreviated forms because these abbreviations have multiple unabbreviated forms.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 52-71 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
The MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.” MPEP 2163.
MPEP § 2163 further states that, for a claimed genus, the written description requirement may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
The claims are drawn to a synthetic capture agent comprising an anchor ligand, a secondary ligand, and a tertiary ligand, wherein the anchor ligand, the secondary ligand, and the tertiary ligand each bind to the same human protein; the anchor ligand comprises 4 or 5 amino acid residues; the secondary ligand and the tertiary ligands each comprise 5 to 7 amino acid residues, wherein the amino acid residues of the secondary ligand or the tertiary ligand are independently selected from the non-natural (D) stereoisomers of the 20 natural amino acids, excluding cysteine and methionine; and the synthetic capture agent further comprises a cell penetrating peptide or a proteosomal degradation tag.
The claims as a whole cover a wide range of capturing agents comprising generic secondary ligand and tertiary ligand; the genus which includes all possible structural characteristics including amino acids and D stereoisomers of said amino acids. Implicit in the claims is that such capture agent must possess certain functional characteristics; namely, the chemical structures bind to any human protein.
The capturing agents meeting the structural requirements of the claims give rise to a large genus that is characterized by substantial variability. Such capturing agents might be proteins, peptides, drugs, modified proteins, or any possible chemical structures including said amino acids and a penetrating peptide or a proteosomal.
Protein chemistry is probably one of the most unpredictable areas of biotechnology. For example, the process of screening for a capture ligand is complicated. Millward et al. (J. Am Chem. Soc. 2011, vol. 133, pp. 18280-18288, IDS submitted 01/13/2025, cite no. C52) disclose a capturing agent comprising anchor, biligand (i.e., secondary), and triligand for Akt (abstract and Schemes 1-3). Millward discloses that “each peptide module in the branched structure makes unique contributions to affinity and/or specificity (abstract). The reference further teaches multi-ligand assembly and requires detailed structural information on the target to guide the screening strategy (p. 18281, left col, last sentence of second para). Millward also teaches a ratio of true hits vs. false positive due to noise (p. 18284, right col., para. 1). Millward also teaches that each biligand linker (4 and 8 carbons) possesses different inhibitory potency. Millward discloses that the longest linker (8 carbons) has a significantly higher inhibitory potency relative to when linker is 4 carbon (p. 18283, right col., para. 3). In other words, the binding affinities of the peptide ligands are significantly affected by as little as 4 carbon molecules. Also, Agnew et al. (US2010/0009896A1, published 01/14/2010, IDS submitted 01/13/2025, cite no. A31) disclose the importance of the functional groups, such as azide and acetylene, interacting on the surface of the target to form a multi-ligand capture agent [0298]. In other words, to be operable in the claimed invention, the genus must possess certain functional characteristics (structure-function relationship) to form and continue to build a multi-ligand capture agent for binding affinity. Thus, it is impossible for one skilled in the art to extrapolate specific examples of compounds of the instant disclosure for Akt to forecast capture agents for either Akt or any human protein.
Meanwhile, the claims encompass a capture agent having endless possibilities of combinations of amino acid residues in forming the claimed synthetic capture agent. The presently claimed genus encompasses an untenable amount of compounds. For instance, the number of compounds embraced by the genus may be roughly estimated to be in the order of > 1035, which all have not been identified as possible ligands for human protein attachments.
However, the specification fails to provide written description for the genus of capturing agents having the claimed generic structures. The specification only discloses ligands of specific short sequences (i.e., 5-7 amino acids, see SEQ ID NOs, Ligands “comprise” do not necessarily have to be short ligands as “comprise” is an open-ended limitation) for binding to a specific protein of Akt2. Meanwhile, the specification discloses the essential process of in situ click chemistry concept for multi-ligand capture agent (see as filed spec. [00160]). However, the specification does NOT provide a clear definition of what defines these amino acid ligands. One skilled in the art would recognize that it is not possible to conclude that any generic capture agents comprising amino acid residues would possess the structure-function relationship to bind to any protein or Akt2. The recited claims encompass ligands of any possible amino acid structures including D stereoisomers, which include structures that hinder binding to Akt2 or any protein. As disclosed by Millward, the binding affinities of peptide ligands are significantly affected by as little as 4 carbon molecules (p. 18283, right col., para. 3). Given the breadth of the claims, the drawings and the examples are not representative of the full scope of the claimed genus. The specification fails to describe the claimed genus such that, for example, each ligand comprises 10 sets of 4-7 amino acid residues and still capable of binding to Akt2.
Thus in the absence of adequate guidance from the specification, undue trial and error experimentation would be required to screen through the myriad of generic chemical ligands against Akt2. The generic invention was not reduced to practice at the time of filing since the artificial sequences only consist of small combinations of short specific sequences for binding to Akt2 and the capture agent is linked by cyclic linkages (for example, 1,2,3-triazole linkages) to position these short amino acids to bind to Akt2. Given the breadth of the claims, unpredictability of the art and lack of guidance in the specification, as discussed above, undue experimentation would be required by one skilled in the art to make or design the claimed capture agent commensurate in scope with the claims.
Thus, the claims do not meet the written description provision of 35 U.S.C. §112(a) or 35 U.S.C. §112 (pre-AIA ), first paragraph.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 52-71 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 52 recites in the preamble that the synthetic capture agent comprising an anchor ligand, a secondary ligand, and a tertiary ligand, but the claim also recites a fourth ligand which is either a cell penetrating peptide or a proteosomal degradation tag. Thus, the claim is unclear to the structure of the synthetic capture agent because is the cell penetrating peptide or a proteosomal degradation tag part of one of these ligands or a fourth ligand attached to the synthetic capture agent. Because the claim is directed to describing the structure of the capture agent, it is unclear to the structure of the capture agent having a cell penetrating peptide or a proteosomal degradation tag. Claims 53-71 are rejected as being dependent from claim 52.
Claim 67 recites “lysosomal-targeting peptide” derived from RNase A, HSC70…are unclear to the structure associated with lysosomal-targeting peptide. In particular, the term “derived from…” does not provide any structure to the phrase lysosomal-targeting peptide. Thus, it is unclear to what is the structure of the lysosomal-targeting peptide.
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 53 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.
Claim 53 is rejected as not being further limiting the subject matter of the synthetic capture agent of claim 52. The recitation of human protein is phosphorylated does not provide any further structural differences of the capture agent between claims 52-53. Regardless of whether the human protein is phosphorylated or not, the structures of the capture agents are the same in a product claim. Thus, the limitations of claim 53 are not further defining the structures of claim 52.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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 52-64, 67-71 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Agnew et al. (US2010/0009896A1, published 01/14/2010, IDS submitted 01/13/2025, cite no. A31).
With regards to claim 52, Agnew teaches multi-ligand capture agents comprising two or more ligands (abstract). Agnew discloses a synthetic capture agent, wherein the capture agent comprises a designed anchor ligand, a designed secondary ligand (see FIG. 6). Agnew teaches the anchor ligand is denoted as 1o and secondary ligand as 2o [0026]. Agnew teaches molecular tags can be built in the capture agent [0178]. Agnew teaches Akt (see FIG. 30c). Agnew teaches non-natural amino acids including D-stereoisomers of naturally occurring amino acids [0071]. Agnew teaches Figs. 5-6 show non-natural amino acids (D-stereoisomers) (also at [0343]). Angew also teaches in Fig. 35a that each X = 18 D-amino acids (no D-cys and no D-met). Agnew teaches additional modifications of the synthesized multi-ligand capture agents can be performed, for example, the multi-ligand capture agent is introduced with a cell-penetrating peptide sequence, which specializes it as a capture agent for targeting and imaging [0180].
Fig. 6 reads on the synthetic capture agent as claimed.
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FIG. 15 reads on the synthetic capture agent as claimed.
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Regarding claim 53, Agnew teaches Akt (see FIG. 30c). Meanwhile, Fig. 15 above would read all the limitations of the claimed structures.
Regarding claim 54, Agnew teaches in Fig. 7 the addition of a propargyl group (i.e., triple bond) at the N-terminus group.
Regarding claims 55-56, Figs. 6 and 15 show that the secondary ligand and tertiary ligand comprise at least 5 amino acid residues. The claims are reciting “open-ended” limitations that would contain additional amino acid residues.
Regarding claim 57, Figs. 6 and 15 show the secondary ligand is covalently linked to the N-terminal of the anchor ligand or the C-terminal of the anchor ligand.
Regarding claims 58-60, Agnew discloses 1,4-substituted-1,2,3-triazole residue [0291] and in Fig. 15 above.
Regarding claims 61-62, Figs. 6 and 15 show the tertiary ligand is covalently linked to the N-terminal of the anchor ligand or the C-terminal of the anchor ligand.
Regarding claims 63-64, Figs. 6 and 15 show the tertiary ligand is covalently linked to the N-terminal of the secondary ligand or the C-terminal of the anchor ligand.
Regarding claims 67-69, Agnew teaches in Fig. 35b that it has a peptide sequence of amino acids AP, which would read on an amino acid sequence of ALAPYIP. Note that the phrase “an” amino acid sequence is interpreted as any portion of the SEQ ID NO: 27. If Applicant intended to recite the entire SEQ ID NO: 27, then it should recite – the amino acid sequence of ALAPYIP –.
Regarding claim 70-71, Agnew teaches in Fig. 15 that the detectable moiety is biotin and biotin-PEG3.
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 52-66 and 70-71 are rejected under 35 U.S.C. 103 as being unpatentable over Agnew et al. (US2010/0009896A1, published 01/14/2010, IDS submitted 01/13/2025, cite no. A31) in view of Su et al. (“Membrane-Bound Dynamic Structure of an Arginine-Rich Cell-Penetrating Peptide, the Protein Transduction Domain of HIV TAT, from Solid-State NMR”, Biochemistry, 2010, pgs. 6009-6020, published 2010).
Agnew has been discussed in the above rejection but the reference does not teach a cell penetrating peptide is HIV-TAT.
Su teaches HIV-1 TAT is an efficient cell-penetrating peptide that diffuses across the lipid membranes of cells despite eight cationic Arg and Lys residues (at abstract). Su further teaches in the abstract that the lack of amphipathic structure is essential for rapid translocation of these Arg-rich cell-penetrating peptides across the lipid membrane without causing permanent damages to the membrane integrity.
Therefore, it would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have used the multi-ligand capture agents as taught by Agnew with HIV-TAT cell-penetrating peptide as taught by Su because Agnew teaches that multi-ligand capture agent is introduced with a cell-penetrating peptide sequence and Su teaches that its HIV-1TAT is an efficient cell penetrating peptide that diffuses across the lipid membranes without causing permanent damages to the membrane integrity.
The person would have a reasonable expectation of success in using HIV-TAT with the multi-ligand capture agent because it has been well understood by Agnew to modify its multi-ligand with a cell-penetrating sequence.
Claims 52-64, and 67-71 are rejected under 35 U.S.C. 103 as being unpatentable over Agnew et al. (US2010/0009896A1, published 01/14/2010, IDS submitted 01/13/2025, cite no. A31) in view of McKnight et al. (US6566088B1, published 05/20/2003, IDS submitted 01/13/2025, cite no. A12)
Agnew has been discussed in the above rejection, but the reference does not teach Hif-1α comprises the amino acid sequence of ALAPYIP (SEQ ID No: 27).
McKnight teaches the synthetic SEQ ID NO: 5 having ALAPYIP of Hif-1α (col. 4, lines 50-57). McKnight further teaches assays may be cell-based (at abstract). McKnight teaches the methods of identifying agents and said methods are amenable to automated, cost-effective high throughput screening of chemical libraries of lead compounds (at col. 2, lines 5-55).
Therefore, it would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have used the multi-ligand capture agents as taught by Agnew with Hif-1α of McKnight because Agnew teaches that multi-ligand capture agent is introduced with a cell-penetrating peptide sequence and McKnight the sequence is for cell-based assays.
The person would have a reasonable expectation of success in using HIV-TAT with the multi-ligand capture agent because it has been well understood by Agnew to modify its multi-ligands with a cell-penetrating sequence for cell-based assays.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 52-71 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-12 of U.S. Patent No. 9239332B2 (‘332) (IDS submitted 01/13/2025, cite no. A6) in view of Agnew et al. (US2010/0009896A1, published 01/14/2010, IDS submitted 01/13/2025, cite no. A31) and Su et al. (“Membrane-Bound Dynamic Structure of an Arginine-Rich Cell-Penetrating Peptide, the Protein Transduction Domain of HIV TAT, from Solid-State NMR”, Biochemistry, 2010, pgs. 6009-6020, published 2010).
Patent No. ‘332 recites a stable, synthetic capture agent that specifically binds Akt, wherein the capture agent comprises an anchor ligand, a secondary ligand, and optionally a tertiary ligand, wherein the capture agent binds to a non-ATP and non-peptide substrate binding site of Akt and wherein the capture agent is capable of allosterically inhibiting Akt activity upon binding to the binding site, wherein said anchor ligand comprises the peptide sequence Az8-VFYRLGY-CONH2 (SEQ ID NO: 17), wherein Az8 represents and azide amino acid having the structure. Patent claim 2 recites Pra-FWFLRG-CONH2 (SEQ ID NO: 18) wherein Pra represents propargylglycine. Patent claim 3 recites tertiary ligand comprises the peptide sequence Ac-C8-RHERI-CONH2 (SEQ ID NO: 19). However, the Patent does not explicitly teach the secondary and tertiary ligands are non-natural D stereoisomers excluding cysteine and methionine and penetrating peptide.
Agnew and Su have been discussed in the above rejection. It would have been obvious to the person at the time of filing to have modified the secondary and tertiary ligands as recited in the Patent to non-natural D stereoisomers as taught by Agnew because Agnew teaches multi-ligands for Akt (i.e., phosphorylated) are using non-natural D stereoisomers and its multi-ligand capture agents are introduced with a cell-penetrating peptide sequence. Additionally, Su teaches that its HIV-1TAT is an efficient cell penetrating peptide that diffuses across the lipid membranes without causing permanent damages to the membrane integrity.
Claims 52-71 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-55 of U.S. Patent No. 11371994B2 (‘994) (IDS submitted 01/13/2025, cite no. A1).
Although the claims at issue are not identical, they are not patentably distinct from each other because Patent No. ‘994 recites a capture agent, wherein the capture agent comprises an anchor ligand, a secondary ligand, and a tertiary ligand, wherein the capture ligand binds to residues 450-481 of phosphorylated Akt2 (i.e., human protein), wherein the anchor ligand comprises an amino acid sequence wkvk (SEQ ID NO:1) or wkvkl (SEQ ID NO:2), wherein the anchor ligand, the secondary ligand, and the tertiary ligand each bind to Akt2, wherein the secondary ligand is identified by contacting an anchor ligand selection block and a plurality of first candidate peptides with Akt2, wherein (a) the anchor ligand selection block comprises the anchor ligand and an azido group and the first candidate peptides each comprise a peptide and an alkynyl group or (b) the anchor ligand selection block comprises the anchor ligand and an alkynyl group and the first candidate peptides each comprise a peptide and an azido group, whereby a biligand is formed by a disubstituted 1,2,3-triazole linkage being formed between the anchor ligand selection block and one of the first candidate peptides by the azido group or alkynyl group of the anchor ligand selection block and the alkynyl group or azido group of the one of the first candidate peptides being brought in close proximity by binding to the Akt2, wherein the candidate peptide with which the triazole linkage is formed with the anchor ligand selection block is identified as the secondary ligand of the capture agent, wherein the peptides of the first candidate peptides comprise 5 to 7 amino acid residues, wherein the amino acid residues are independently selected from the non-natural (D) sterioisomers of the 20 natural amino acids, excluding cysteine and methionine, wherein the tertiary ligand is identified by contacting a biligand selection block and a plurality of second candidate peptides with Akt2, wherein (a) the biligand selection block comprises the biligand and an azido group and the second candidate peptides each comprise a peptide and an alkynyl group or (b) the biligand selection block comprises the biligand and an alkynyl group and the second candidate peptides each comprise a peptide and an azido group, whereby a triligand is formed by a disubstituted 1,2,3-triazole linkage being formed between the biligand selection block and one of the second candidate peptides by the azido group or alkynyl group of the biligand selection block and the alkynyl group or azido group of the one of the second candidate peptides being brought in close proximity by binding to the Akt2, wherein the candidate peptide with which the triazole linkage is formed with the biligand selection block is identified as the tertiary ligand of the capture agent, wherein the peptides of the second candidate peptides comprise 5 to 7 amino acid residues, wherein the amino acid residues are independently selected from the non-natural (D) sterioisomers of the 20 natural amino acids, excluding cysteine and methionine. Patent claim 14 recites the capture agent further comprises a cell penetrating peptide. Patent claim 15 recites the cell penetrating peptide is HIV-TAT. Patent claim 38 recites the tag is the Hif-1α degradation peptide ALAPYIP (SEQ ID NO:27).
Claims 52-71 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-22 of U.S. Patent No. 10975123B2 (‘123) (IDS submitted 01/13/2025, cite no. A3).
Although the claims at issue are not identical, they are not patentably distinct from each other because Patent No. ‘123 recites a capture agent that binds a variant Akt1 protein, wherein the variant Akt1 protein has been mutated from a glutamate to a lysine at position 17, wherein the capture agent comprises an anchor ligand, a secondary ligand, and optionally, a tertiary ligand, wherein the anchor ligand specifically binds the variant Akt1, wherein the anchor ligand comprises an amino acid sequence yleaf (SEQ ID NO: 43), wherein the secondary ligand is identified by contacting an anchor ligand selection block and a plurality of first candidate peptides with the variant Akt1 protein, wherein (a) the anchor ligand selection block comprises the anchor ligand and an azido group and the first candidate peptides each comprise a peptide and an alkynyl group or (b) the anchor ligand selection block comprises the anchor ligand and an alkynyl group and the first candidate peptides each comprise a peptide and an azido group, wherein the candidate peptides comprise five amino acids each randomly selected from 18 D-stereoisomers of the natural amino acids, minus Cysteine and Methionine, whereby a biligand is formed by a disubstituted 1,2,3-triazole linkage being formed between the anchor ligand selection block and one of the first candidate peptides by the azido group or alkynyl group of the anchor ligand selection block and the alkynyl group or azido group of the one of the first candidate peptides being brought in close proximity by binding to the variant Akt1 protein, wherein the candidate peptide with which the triazole linkage is formed with the anchor ligand selection block is identified as the secondary ligand of the capture agent, wherein the tertiary ligand is identified by contacting a biligand selection block and a plurality of second candidate peptides with the variant Akt1 protein, wherein (a) the biligand selection block comprises the biligand and an azido group and the second candidate peptides each comprise a peptide and an alkynyl group or (b) the biligand selection block comprises the biligand and an alkynyl group and the second candidate peptides each comprise a peptide and an azido group, wherein the candidate peptides comprise five amino acids each randomly selected from 18 D-stereoisomers of the natural amino acids, minus Cysteine and Methionine, whereby a triligand is formed by a disubstituted 1,2,3-triazole linkage being formed between the biligand selection block and one of the second candidate peptides by the azido group or alkynyl group of the biligand selection block and the alkynyl group or azido group of the one of the second candidate peptides being brought in close proximity by binding to the variant Akt1 protein, wherein the candidate peptide with which the triazole linkage is formed with the biligand selection block is identified as the tertiary ligand of the capture agent. Patent claim 10 recites the capture agent further comprises a cell penetrating peptide. Patent claim 11 recites the cell penetrating peptide is HIV-TAT. Patent claim 18 recites a tag that comprises the amino acid sequence ALAPYIP (SEQ ID NO: 93).
Conclusion
No claim is allowed.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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