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 .
Applicant’s election without traverse of group I, claims 1-9 and 13-14 in the reply filed on 3/6/26 is acknowledged.
Claims 15-23 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 3/6/26.
Claims 1-9 and 13-14 are under examination.
Nucleotide and/or Amino Acid Sequence Disclosures
Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures
37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted:
1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying:
a. the name of the XML file
b. the date of creation; and
c. the size of the XML file in bytes; or
2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying:
a. the name of the XML file;
b. the date of creation; and
c. the size of the XML file in bytes.
SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS:
Specific deficiency - Sequences appearing in the specification are not identified by sequence identifiers (i.e., “SEQ ID NO:X” or the like) in accordance with 37 CFR 1.831(c). See pages 10 and 33
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers, consisting of:
• A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
• A copy of the amended specification without markings (clean version); and
• A statement that the substitute specification contains no new matter.
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 1-9 and 13-14 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 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.”
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, 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 Applicants were in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
The instant claims are drawn to an isolated peptide comprising or consisting of the amino acid sequence,
(GHGXY)n K (GHGXY)mZ,
(GHGXY K)n (GHGXY)mZ, or
(GHGXY)n (K GHGXY)mZ,
wherein
X is valine (V), leucine (L) or proline (P),
Z is tryptophan (W) or absent,
nis0, 1, 2, 3, 4 or 5, m is 0, 1, 2, 3, 4or 5, and
n+m is 3, 4 or 5, preferably 5.
The specification teaches that that engineered artificial peptides derived from histidine-rich beak peptide (HBpep) that additionally comprise a lysine residue (K) between the pentapeptide repeats or at the termini of such a peptide provide for a means to overcome the previous drawback of delayed or impaired intracellular release of the cargo from a coacervate formed by these peptides. The specification discloses the isolated peptide (HBpep-K) sequence comprising the amino acid sequence GHGVY GHGVY GHGPY K GHGPY GHGLY W (SEQ ID NO: 10) with insertion of a single lysine residue (K) at position 16 from the N-terminal of HBpep was used as the representative isolated peptide sequence in the peptide coacervate composition. NHS- SS-Ac and NHS-SS-Ph, synthesized from acetic acid (Ac) and benzoic acid (Ph), respectively, were used as representative self-immolative (SR) moieties.
The issue with regards to the written description provision of 112(a) is that the claims encompass a genus of peptides that is not adequately described. The specification discloses the isolated peptide set forth in SEQ ID NO: 10 comprising five histidine residues, a lysine at position 16, and the self-immolative moieties NHS- SS-Ac or NHS-SS-Ph. However, the claims are not limited to this species, and instead, broadly encompass peptides having any variation of the claimed sequences that differ in histidine content, lack a lysine residue, and lack a self-immolative moiety form the single species disclosed. This, indicates there are hundreds, if not thousands, of peptides encompassed by the claims. For example, an isolated peptide having the sequence (GHGXY K)n (GHGXY)mZ wherein n = 0 and m=3 would contain no lysine and three histidine residues. These peptides have no correlation between their structure and function. The peptides have the required function of forming a coacervate for intracellular delivery and direct cytosolic release of an active agent, and the specification teaches that a lysine is required for the formation of coacervates, i.e., phase separate, at an increased pH of 9.0, and remain as monomeric peptides in solution at near neutral conditions, i.e., pH of about 5.0 to 8.0. However, with the exception of the isolated peptide set forth in SEQ ID NO: 10 comprising a lysine at position 16, and the self-immolative moieties NHS- SS-Ac or NHS-SS-Ph, the specification does not disclose any peptide that has a different histidine content, and lacks a lysine and self-immolative moiety that has the required function. Therefore, the specification does not provide adequate written description to identify the broad genus of the claims because, inter alia, the specification does not disclose a correlation between the necessary structure of the peptide comprising an amino acid sequence having less than five histidine residues, no lysine residues, and no self-immolative moiety and the claimed function to be maintained (e.g., form a coacervate).
Furthermore, Applicants have not shown a representative number of species that have the claimed function. While the specification clearly sets forth a correlation between the isolated peptide having the amino acid sequence set forth in SEQ ID NO: 10 comprising a lysine at position 16, and the self-immolative moieties NHS- SS-Ac or NHS-SS-Ph, and the claimed function (i.e., forming a coacervate), this correlation does not appear to be clearly present in the breadth of the claims. As noted above, the claims are not limited to the isolated peptide set forth in SEQ ID NO: 10 conjugated to a self-immolative moiety and encompass peptides comprising an amino acid sequence having less than five histidine residues, no lysine residues, and no self-immolative moiety. Thus, the genus has substantial variation because of the numerous alternatives and combinations permitted. There is no description of the structure common to the members of the genus such that one of skill in the art can visualize or recognize the members of the genus. Therefore, only a single species has been described and this is not considered to be representative of the breadth of the genus.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that "applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed." (See page 1117.) The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116.)
With the exception of the isolated peptide set forth in SEQ ID NO: 10 conjugated to a self-immolative moiety, the skilled artisan cannot envision the detailed chemical structure of the encompassed agents, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The nucleic acid and/or protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601,1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481,1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
Finally, University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that: ...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines Inc., 107 F.3d 1565, 1572, 41 USPQ2dl961,1966 (1997); In re Gosteli, 872 F.2dl008,1012,10 USPQ2dl614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d 1966.
The state of the art regarding peptide coacervates is discussed by Gabryelczyk et al. ((2019). Hydrogen bond guidance and aromatic stacking drive liquid-liquid phase separation of intrinsically disordered histidine-rich peptides. Nature Communications, 10(1), Article 5465). Gabryelczyk et al. teach that HBPs (histidine-rich beak proteins) are characterized by the presence of repetitive regions of low complexity amino acid sequence in their C-termini (See page 2). Gabryelczyk et al. teach that HBP-1 sequence contains the motif repeat GHGLY that drives LLPS (coacervation) (See page 2). Gabryelczyk et al. teach that when at least two copies of such repeats and a linker sequence are included, LLPS can be induced over a broader range of conditions (pH and salt concentration) (See page 2). Gabryelczyk et al. teach that shorter fragments of HBP-2 comprising the GHGxY motif were tested for the ability to coarcervate and only the C-terminal fragment (A83-R172) phase-separated into coacervates (See page 5). Gabryelczyk et al. teach that shorter peptides of HBP-1 and HBP2 were analyzed for separation behavior (See page 5). Gabryelczyk et al. teach that phase separation was observed for all 25-mer peptides containing two GHGLY motifs flanking the central region composed of three copies of GAGFA or GHGLH sequences, as well as for a 20-mer peptide (GY-20) made of four copies of GHGLY motif arranged as tandem repeats (See page 5). Gabryelczyk et al. teach that no phase separation was observed when the peptide length was reduced to 15 amino acids, for example when three copies of GHGLY motif were arranged in tandem (GY-15-V1) or when the GAGFA motif was flanked by GHGLY (GY-15-V2). Gabryelczyk et al. teach that similarly, no phase separation was observed for decapeptides composed of one or two GHGxY motifs or for pentapeptides GHGLY or GAGFA, respectively (See page 5). Gabryelczyk et al. teach these results indicate that when at least two copies of the GHGLY motif are present in the tandem repeats, the phase separation ability is greatly enhanced. However, this condition is not sufficient and GHGLY copies must additionally be separated by a spacer composed of at least three copies of GAGFA or GHGLH motifs, or a combination of GAGFA/GFA and GHGLH motifs. Alternatively, the peptide must contain at least four tandem repeats of GHGLY motif to phase separate (See page 5). Thus, the art makes clear that specific structural conditions must be met for the peptide to have the ability to coacervate.
Furthermore, it is well known that protein folding and formulation are complex and fairly unpredictable processes, in such that substituting even one amino acid within the sequence can change the structure and function of said protein. Punta et al. (PLoS Comput Biol 4(10): e1000160, 2008) teach that relatively small difference in sequence can sometimes cause quite radical changes in functional properties, such as a change of enzymatic action, or even loss or acquisition of enzymatic activity itself (See page 2). Punta et al. teach that it is also apparent that there is no sequence similarity threshold that guarantees that two proteins share the same function (see page 2). Punta et al. teach that homology between two proteins does not guarantee that they have the same function, not even when sequence similarity is very high (including 100% sequence identity) (See page 2 and table 2). Punta et al. teach that proteins live and function in 3D, and therefore structural information is very helpful for predicating function (See page 4). However, as with sequence, two proteins having the same overall architecture, and even conserved functional residues, can have unrelated functions (See page 4). Punta et al. teach that still; structural knowledge is an extremely powerful tool for computational function prediction (See page 5).
The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al. (J. Cell Biol. 111:2129-2138, 1990) who teach that replacement of a single lysine reside at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Song et al. (Molecular Biology of the Cell, 15:1287–1296, March 2004) who teach that substitution of alanine for aspartate in survivin results in the conversion of survivins’ apoptotic function from anti-apoptotic to proapoptotic and changes in its subcellular localization (See page 1287-1289). Moreover, Defeo-Jones et al. (Molecular and Cellular Biology, Sept. 1989, p. 4083-4086) teach that the conservative substitution of lysine for arginine at position 42 completely eliminated biological activity (See abstract and pages 4084-4085). These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein.
Additionally, Bork (Genome Research, 2000; 10:398-400) clearly teaches the pitfalls associated with comparative sequence analysis for predicting protein function because of the known error margins for high-throughput computational methods. Bork specifically teaches that computational sequence analysis is far from perfect, despite the fact that sequencing itself is highly automated and accurate (p. 398, column 1). One of the reasons for the inaccuracy is that the quality of data in public sequence databases is still insufficient. This is particularly true for data on protein function. Protein function is context dependent, and both molecular and cellular aspects have to be considered (p. 398, column 2). Conclusions from the comparison analysis are often stretched with regard to protein products (p. 398, column 3). Further, although gene annotation via sequence database searches is already a routine job, even here the error rate is considerable (p. 399, column 2). Most features predicted with an accuracy of greater than 70% are of structural nature and, at best, only indirectly imply a certain functionality (see legend for table 1, page 399). As more sequences are added and as errors accumulate and propagate it becomes more difficult to infer correct function from the many possibilities revealed by database search (p. 399, paragraph bridging columns 2 and 3). The reference finally cautions that although the current methods seem to capture important features and explain general trends, 30% of those features are missing or predicted wrongly. This has to be kept in mind when processing the results further (p. 400, paragraph bridging cols 1 and 2).
Given not only the teachings of Punta et al., Song et al., Burgess et al., and Defeo-Jones et al., but also the limitations and pitfalls of using computational sequence analysis and the unknown effects of alternative splicing, post translational modification and cellular context on protein function as taught by Bork, the claimed polynucleotides having the required function(s) could not be predicted based on sequence identity. Clearly, it could not be predicted that a peptide that shares only partial homology with a disclosed sequence or that is a fragment of a sequence will function in a given manner. Therefore, the state of the art supports that even the skilled artisan requires guidance on the critical structures of the peptide sequences per se and thereby does not provide adequate written description support for which structural features of any given peptide sequence and resultant polypeptide would predictably retain their functional activities.
Applicant is reminded that generally, in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus (Enzo Biochem, Inc. v. Gen- Probe Inc., 323 F.3d 956 (Fed. Cir. 2002); Noelle v. Lederman, 355 F.3d 1343 (Fed. Cir. 2004); Regents of the University of California v. Eli Lilly Co., 119 F.3d 1559 (Fed. Cir. 1997)). A patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017) at page 1358). An adequate written description must contain enough information about the actual makeup of the claimed products — “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361).
Adequate written description requires more than a mere statement that is part of the invention. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. v. Chungai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
The University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404, 1405 held that: ...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that “the inventor invented the claimed invention.” Lockwood v. American Airlines Inc. 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) ("[T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus an Applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2dat1966.
MPEP § 2163.02 states, “[a]n objective standard for determining compliance with the written description requirement is, ‘does the description clearly allow person of ordinary skill in the art to recognize that he or she invented what is claimed’”. The courts have decided: the purpose of the “written description" requirement is broader than to merely explain how to "make and use"; the Applicant must convey with reasonable clarity to those skilled in the art, that as of the filing date sought, he or she was in possession of the invention. The invention is for purposes of the “written description” inquiry, whatever is now claimed. See Vas-Cath, Inc v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Federal Circuit, 1991).
Furthermore, the written description provision of 35 USC §112 is severable from its enablement provision; and adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993). And Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. Moreover, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. However, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; nor has Applicant shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; nor has the Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed.
Therefore, for all these reasons the specification lacks adequate written description, and one of skill in the art cannot reasonably conclude that Applicant had possession of the claimed invention at the time the instant application was filed.
These peptides have no correlation between their structure and their function.
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 1-9 and 13-14 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.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 recites the broad recitation “n+m = 3, 4, or 5”, and the claim also recites “preferably 5” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims. The dependent claims do not cure the deficiencies of claim 1, and thus, are included in the rejection.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 6 recites the broad recitation “C6-aryl”, and the claim also recites “phenyl” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
Claim 8 recites the limitation "the self-immolative moiety" in line 2. There is insufficient antecedent basis for this limitation in the claim. Claim 8 depends from claim 7, and there is no recitation of a self-immolative moiety in claim 7. Clarification and/or correction is required.
Claim 9 is indefinite because of the use of parentheses. Although parenthesis may be appropriate when defining an abbreviation or acronym, the inclusion of parentheses for anything else (e.g. “(poly)peptides” and “(small) chemical compounds”), raises uncertainty as to whether the feature in the parentheses is optional or always present. Thus, clarification of the claim is required to ascertain the metes and bounds.
Claim Rejections - 35 USC § 102
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.
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.
(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.
Claim(s) 1, 7, 9, and 13-14 is/are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Miserez et al. (US Patent Application Publication 2019/0388357 A1, published December 26, 2019).
The instant claims are drawn to an isolated peptide comprising or consisting of the amino acid sequence,
(GHGXY)n K (GHGXY)mZ,
(GHGXY K)n (GHGXY)mZ, or
(GHGXY)n (K GHGXY)mZ,
wherein
X is valine (V), leucine (L) or proline (P),
Z is tryptophan (W) or absent,
nis0, 1, 2, 3, 4 or 5,m is 0, 1, 2, 3, 4or 5, and
n+m is 3, 4 or 5, preferably 5.
Miserez et al. teach a composition for delivery of an active agent, the composition comprising a peptide coacervate, wherein the peptide coacervate comprises the sequence of GHGXY GHGXY GHGXY GHGXY GHGXY W (SEQ ID NO: 3), which reads on the peptide sequence of (GHGXY K)ₙ=0 (GHGXY) Z recited in claim 7, wherein X is valine, leucine, or proline, n ≥ 4, (See claim 6 and paragraph 0015-0017 and 0030). Miserez et al. teach a peptide coacervate comprising the sequence GHGXY GHGXY GHGXY GHGXY GHGXY, which reads on the peptide sequence of (GHGXY K)n (GHGXY)mZ, wherein n=0, m=5, and Z is absent (See claim 7 and paragraph 0139). Miserez et al. teach that the active agent is selected from the group consisting of proteins, (poly)peptides, carbohydrates, nucleic acids, lipids, chemical compounds, nanoparticles, and combinations thereof (See claim 9). Miserez et al. teach that the active agent is a pharmaceutical of diagnostic agent (See claim 10). Miserez et al. teach that the pH of the composition is >7.0 and <10 (See claim 16 and paragraphs 0035-0038). Thus, Miserez et al. anticipate the claims.
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.
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Claims 1, 7, 9, and 13-14 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5, 6, 7, 9, 10, 13, and 16 of U.S. Patent No. 11,179,342. Although the claims at issue are not identical, they are not patentably distinct from each other because both sets of claims are drawn to an isolated peptide comprising the amino acid sequence of (GHGXY)n K (GHGXY)mZ, (GHGXY K)n (GHGXY)mZ, or (GHGXY)n (K GHGXY)mZ,
wherein X is valine (V), leucine (L) or proline (P), Z is tryptophan (W) or absent, n is 0, 1, 2, 3, 4 or 5, m is 0, 1, 2, 3, 4or 5, and n+m is 3, 4 or 5, preferably 5.
The ‘342 claims teach a composition for delivery of an active agent, the composition comprising a peptide coacervate, wherein the peptide coacervate comprises: one or more peptides derived from histidine-rich proteins; and an active agent encapsulated in the peptide coacervate. The ‘342 claims teach wherein the peptides derived from histidine-rich proteins are fragments of DgHBP-1 and/or DgHBP-2 that comprise at least one copy of the peptide motif GHGXY, wherein X is valine (V), leucine (L) or proline (P). The ‘342 claims teach wherein the peptides derived from histidine-rich proteins comprise an amino acid sequence selected from the group consisting of: (GHGXY)n, wherein X is valine (V), leucine (L), or proline (P), and n is ≥4. It should be noted that the sequence (GHGXY)n, wherein X is valine (V), leucine (L), or proline (P), and n is ≥4, reads on the claimed (GHGXY K)n (GHGXY)mZ, wherein n =0, m=4, and Z is absent. The ‘342 claims teach wherein the peptides derived from histidine-rich proteins comprise an amino acid sequence selected from the group consisting of: (i) (SEQ ID NO: 3) GHGXY GHGXY GHGXY GHGXY GHGXY W and (ii) (SEQ ID NO: 4) GHGXY GHGXY GHGXY GHGXY GHGXY. The ‘342 claims teach wherein the active agent is selected from the group consisting of proteins, (poly)peptides, carbohydrates, nucleic acids, lipids, chemical compounds, nanoparticles, and combinations thereof. The ‘342 claims teach wherein the composition is a pharmaceutical or diagnostic formulation for administration to a subject. The ‘342 claims teach wherein the pH of the composition is >7.0 and <10. Thus, the ‘342 claims anticipate the instant claims, and the instant claims and the ‘342 claims are not patentably distinct.
Claim Status
No claims are allowed.
Conclusion
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/SANDRA CARTER/Examiner, Art Unit 1674
/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674
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