Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Species A (i.e., a single and specific hydrophobic peptide as one according to General Formula I in which Xaa1 is L-Ala and m is 10, and the peptide is a rod-shaped having an alpha-helix structure); Species B (i.e., a single and specific peptide complex as Species A complexed to PEG as a hydrophilic polymer and one positively charge amino acid residue that is arginine, and the structure of a vesicle); and Species C (i.e., a single and specific composition as Species B and ssDNA that is a short oligomer with a length of 20 nucleotides of SEQ ID NO: 120 as the nucleic acid material, and a nanostructure) in the reply filed on June 3, 2026, is acknowledged.
Please note that for Species A, election of “m”, and the number of positively charged amino acids is hereby withdrawn; and Xaa1 is expanded to include L-Leu in light of the search results. Also please note that for Species B, election of a single and specific nucleic acid material is hereby removed.
Status of Claims
Claims 1-23 were originally filed on June 11, 2024.
Claims 1-23 are currently pending and claims 1-9, 13, 15, and 18-23 are under consideration as claims 10-12, 14, and 16-17 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on June 3, 2026.
Priority
The present application claims priority under 119(a)-(d) to Korean Application No. 10-2022-0162494 filed on November 29, 2022.
Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d) for Korean Application No. 2022-0162494, which papers have been placed of record in the file. Please note that the Korean application is NOT in English and therefore cannot be verified.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on November 22, 2023; March 5, 2025; and October 31, 2025, are being considered by the examiner.
Sequence Interpretation
For claim 1, please note that the Examiner is interpreting the scope as open-ended requiring 100% identity to elected General Formula I where Xaa1 is L-Ala and m is 4-50, but where the sequence encompasses any N- and/or C-terminal additions as long as the overall function of the peptide remains hydrophobic.
Sequence Compliance
Applicant is advised that the application is not in compliance with 37 CFR §§ 1.821-1.825.
This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR § 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 CFR §§ 1.821-1.825 for the reason(s) set forth below. Applicant must comply with the requirements of the sequence rules (37 CFR §§ 1.821- 1.825) in order to completely respond to this office action.
Specifically, claim 1 is directed to a hydrophobic peptide represented by General Formula I or 2 where General Formula 1 is –{[Aib]-[Xaa1]}m- and General Formula 2 is Xaa1-{[Aib]-[Xaa1]}m- where m is 4-50. Although Xaa1 is variable, when considering m is 4-50, the peptide has a minimum sequence of -[Aib]-[Xaa1]-[Aib]-[Xaa1]-[Aib]-[Xaa1]-[Aib]-[Xaa1]- . As such, the minimum sequence contains at least four defined residues, i.e., Aib. Thus, each formula requires a sequence identifier because they require at least 4 defined amino acid residues.
Furthermore, it is noted that withdrawn claim 14 is directed to where the positively charged peptide is any one selected from SEQ ID NOs: 139-150. However, the sequence listing received on 11/22/23 only has a total of 122 sequences. Therefore, there are no identifiable SEQ ID NOs: 139-150. However, it is noted that the specification refers to SEQ ID NOs: 108-119 as positively charged peptides.
Moreover in the specification on pg. 28, 7th paragraph, reference to RGD sequences is made. It is noted that every occurrence of a sequence with at least 4 defined residues should be accompanied with a sequence identifier. Even if the sequence has been identified in another section of the specification, the repeat sequence identifier should be reiterated.
In order to satisfy the sequence rules requirements, Applicant needs to provide an amendment to the instant claims and specification to include reference to the appropriate sequence identifier “SEQ ID NO:” in parenthesis next to each of the sequences having 4 or more amino acids. Please confirm that all peptides having 4 or more than 4 amino acid residues have sequence identifiers and are included in the sequence listing.
In case of any new sequences not properly identified in the instant specification, Applicant is required to provide a substitute computer readable form (CRF) copy of a “Sequence Listing” which includes all of the sequences that are present in the instant application and encompassed by these rules, a new or substitute paper copy of that “Sequence Listing”, an amendment directing the entry of that paper copy into the specification, and a statement that the content of the paper and computer readable copies are the same and, where applicable, include no new matter, as required by 37 C.F.R. § 1.821(e) or 1.821(f) or 1.821(g) or 1.825(d). The instant specification will also need to be amended so that it complies with 37 C.F.R. § 1.821(d) which requires a reference to a particular sequence identifier (SEQ ID NO:) be made in the specification and claims wherever a reference is made to that sequence. For rules interpretation Applicant may call (571) 272-2533. See M.P.E.P. 2422.04.
Please direct all replies to the United States Patent and Trademark Office via one (1) of the following:
1. Electronically submitted through EFS-Bio (<http://www.uspto.gov/ebc/efs/downloads/documents.htm>, EFS Submission User Manual - ePave)
2. US Postal Service:
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PO Box 22313-1450
Alexandria, VA 22313-1450
3. Hand carry, Federal Express, United Parcel Service, or other delivery service:
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Drawings
Figures 37-39, and 42C-D are objected to because they depict amino acid sequences/structures without including SEQ ID NOs for each of the sequences. However, the SEQ ID NOs: need to be present in either the figure or the Brief Description of the Drawings.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
The drawings; in particular, Figure 42A-B, 42F, 44A, 44I, 49I, and 50, are objected to because of the following reason:
The drawings have a line quality that is too light to be reproduced (weight of all lines and letters must be heavy enough to permit adequate reproduction) or text that is illegible (reference characters, sheet numbers, and view numbers must be plain and legible) see 37 CFR 1.84(l) and (p)(1)); See Figure(s) 42A-B, 42F, 44A, 44I, 49I, 50.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Rejections - 35 USC § 112
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.
Claim 15 is 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. Regarding claim 15, the phrase "such as" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Please note that the Examiner is interpreting the scope of claim 15 such that the peptide complex self-assembles into a spherical nanoparticle wherein the spherical nanoparticle is selected from a micellar structure and a vesicular structure in solution, in order to advance prosecution.
Claim 19 is 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 pre-AIA the applicant regards as the invention. In the instant case, claim 19 is directed to “…a nanostructure having an artificial chromosome-like structure via noncovalent bonding.” Pursuant to MPEP 2173.05(b)(II), the addition of the word “like” to an otherwise definite term of chromosome extends the scope of a chromosome structure so as to render it indefinite. Accordingly, referring to an artificial chromosome-like structure is indefinite.
Please note that the Examiner is interpreting the scope of claim 19 such that the nanostructure has an artificial chromosome structure via noncovalent bonding in order to advance prosecution.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1-8 and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Miura et al., Langmuir 14:2761-2767 (1998).
For claims 1-5, Miura et al. discloses the hydrophobic alpha-helix self-assembly peptide with the structure:
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(i.e., Aib-(L-Ala-Aib)8) (See Miura, abstract; Figure 2). When considering the full structure of Miura’s peptide, the peptide also has the general formula –(Aib-L-Ala)8-Aib, i.e., shift the parentheses by one to the left. As discussed in the “Sequence Interpretation” section supra, the scope of the claimed peptide of claim 1 encompasses additional N- and/or C-terminal residues as long as the peptide maintains its hydrophobic nature. Since the additional residue at the C-terminus is Aib, Miura’s peptide would maintain its hydrophobic nature. Thus, Miura’s peptide constitutes a specific species of a peptide of instant General Formula I where Xaa1 is Ala and m is 8 as recited in instant claims 1-5.
With respect to the peptide being hydrophobic, as discussed supra, Miura expressly teaches that the peptide is hydrophobic in nature. However, the physical property (i.e., being hydrophobic) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new physical property (i.e., being hydrophobic) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Thus, Miura’s disclosure satisfies the claim limitations as recited in instant claims 1-5.
For claim 6, as discussed supra, Miura et al. discloses that the peptides form an alpha-helix structure (See Miura, pg. 2761, col. 1, 1st to last paragraph). Miura et al. does not expressly teach that the peptides is a rod-shaped hydrophobic peptide. However, given that Miura et al. discloses a specific species of peptide having the claimed structure of General formula I, the physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of new physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) which are inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Thus, Miura’s disclosure satisfies the claim limitations as recited in instant claim 6.
For claim 7, Miura et al. does not expressly disclose that the peptide is controlled to be arranged and oriented in the direction of an external magnetic field. Rather, Miura et al. formed a self-assembled monolayer (SAM) on a gold surface such that the alpha-helical peptides are nearly perpendicular to the substrate surface as depicted in Figure 1 via complex formation with 18-Crown-6-ether and noncovalent linkage to either 2-aminoethanethiol HCl or N-(Ɛ-amino-caproyl)-2-aminoethyl disulfide HCl (See Miura, pg. 2762, col. 1, last paragraph to col. 2, 1st paragraph; Figure 1-3). However, it is unnecessary for a prior art reference to teach this limitation because an intended use of the peptide (i.e., being controlled to be arranged and oriented in the direction of an external magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the peptide being controlled to be arranged and oriented in the direction of an external magnetic field is an intended use of the claimed peptide that gives little meaning and purpose to the structure of the claimed peptide. In other words, the claim is directed to the structure of a peptide and not a device or substrate surface that includes the structure of a magnetic field. Accordingly, claim 7 recites an intended use that does not render material to patentability.
For claim 8, Miura et al. formed a self-assembled monolayer (SAM) on a gold surface such that the alpha-helical peptides are perpendicular to the substrate surface as depicted in Figure 1 via complex formation with 18-Crown-6-ether and noncovalent linkage to either 2-aminoethanethiol HCl or N-(Ɛ-amino-caproyl)-2-aminoethyl disulfide HCl (See Miura, pg. 2762, col. 1, last paragraph to col. 2, 1st paragraph; Figure 1-3). The structure of two species depicted in Figure 2 as:
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(See Miura, Figure 2). In these species, the general formula is (Aib-L-Ala)8-Aib-L-Ala-(18-Crown-6-ether). As such, these peptide species constitute a hydrophobic peptide of general formula I as recited in instant claim 1. It is further noted that the instant specification defines a polymer as referring to a macromolecule having repeat units linked by covalent bonds (See instant, pg. 14, 9th paragraph). As such, 18-Crown-6-ether constitutes a polymer as recited in instant claim 8, which contains a hydrophilic core. Since 18-Crown-6-ether has a hydrophilic core and there is no structural requirement that the hydrophilic core is directly bound to one or both ends of the hydrophobic peptide, Miura’s peptides constitute a peptide complex as recited in instant claim 8.
For claim 15, Miura et al. does not expressly disclose that the peptide complex self-assembles into a spherical nanoparticle such as a vesicular structure in solution. Rather, Miura et al. formed a self-assembled monolayer (SAM) on a gold surface (See Miura, pg. 2762, col. 1, last paragraph to col. 2, 1st paragraph; Figure 1-3). As such, Miura et al. did not evaluate the structure of the peptide complex in solution. However, it is unnecessary for a prior art reference to teach this limitation because a physical/structural property of the peptide (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, given that Miura et al. discloses specific species of peptides having the claimed structure of General formula I, the physical/structural property of the peptide (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) is an intended result of the claimed peptide that gives little meaning and purpose to the structure of the claimed peptide. Accordingly, claim 15 recites an intended result that does not render material to patentability.
Accordingly, Miura’s disclosure anticipates instant claims 1-8 and 15.
Claims 1-8, 15, 18, 20 and 22-23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Itagaki et al., Chimia 72:842-847 (2018).
For claims 1-3, 8 and 18, Itagaki et al. discloses membrane-based self-assembly of the organic nanotubes using amphiphilic polypeptides of poly(sarcosine) b-(L- or D-Leu-Aib)n (n = 6–8) (See Itagaki, pg. 842, col. 1, 1st paragraph). For example, poly(sarcosine)-b-(L-Leu-Aib)6 self-assembled into curved sheets just after injection into water, which converted to nanotubes upon heating at 90 °C (See Itagaki, pg. 842, col. 1, 1st paragraph). A specific species of peptide complex is:
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(See Itagaki, Figure 1). The peptide component, i.e., (L-Leu-Aib)6 would correlate to a peptide with the general formula of L-Leu-(Aib-L-Leu)5-Aib where the C-terminus is modified with -OCH3 and the N-terminus is complexed with poly(sarcosine), which constitutes a hydrophilic polymer. Then adenine is conjugated to the N-terminal end of the poly(sarcosine) as a nucleobase. It is noted that the instant specification does not define what constitutes nucleic acid material. Since adenine is a building block of nucleotides, it would broadly constitute a nucleic acid material.
With respect to the peptide being hydrophobic, as discussed supra, Itagaki et al. expressly teaches that the peptide is hydrophobic in nature. However, the physical property (i.e., being hydrophobic) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new physical property (i.e., being hydrophobic) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977).
With respect to where the composition is for safely storing nucleic acid information, pursuant under MPEP 2111.02(II):
statements in the preamble reciting the purpose or intended use of the claimed invention must be evaluated to determine whether or not the recited purpose or intended use results in a structural difference (or, in the case of process claims, manipulative difference) between the claimed invention and the prior art. If so, the recitation serves to limit the claim. See, e.g., In re Otto, 312 F.2d 937, 938, 136 USPQ 458, 459 (CCPA 1963) (The claims were directed to a core member for hair curlers and a process of making a core member for hair curlers. The court held that the intended use of hair curling was of no significance to the structure and process of making.); In re Sinex, 309 F.2d 488, 492, 135 USPQ 302, 305 (CCPA 1962) (statement of intended use in an apparatus claim did not distinguish over the prior art apparatus). To satisfy an intended use limitation which is limiting, a prior art structure which is capable of performing the intended use as recited in the preamble meets the claim. See, e.g., In re Schreiber, 128 F.3d 1473, 1477, 44 USPQ2d 1429, 1431 (Fed. Cir. 1997) (anticipation rejection affirmed based on Board’s factual finding that the reference dispenser (a spout disclosed as useful for purposes such as dispensing oil from an oil can) would be capable of dispensing popcorn in the manner set forth in appellant’s claim 1 (a dispensing top for dispensing popcorn in a specified manner)) and cases cited therein. (emphasis added).
As such, a composition is intended to be used to safely store nucleic acid information. Thus, the claimed composition being used to safely store nucleic acid information is the intended use of the composition. Although Itagaki et al. does not expressly disclose that the composition is used to safely store nucleic acid information, the composition is capable of performing the claimed intended use, i.e., being used to safely store nucleic acid information.
Thus, the specific species disclosed by Itagaki et al. constitutes a hydrophobic peptide represented by instant General Formula I where Xaa1 is L-Leu and m is 5 as recited in instant claims 1-3, a peptide complex comprising the peptide of claim 1 and a hydrophilic polymer bound to one end of the peptide as recited in instant claim 8, and a composition for safely storing nucleic acid information comprising the peptide complex of claim 8 and a nucleic acid material as recited in instant claim 18.
For claims 4-5, as discussed supra, Itagaki et al. discloses membrane-based self-assembly of the organic nanotubes using amphiphilic polypeptides of poly(sarcosine) b-(L- or D-Leu-Aib)n (n = 6–8) (See Itagaki, pg. 842, col. 1, 1st paragraph). Pursuant to MPEP 2131.02, it states that, “[i]f one of ordinary skill in the art is able to "at once envisage" the specific compound within the generic chemical formula, the compound is anticipated. One of ordinary skill in the art must be able to draw the structural formula or write the name of each of the compounds included in the generic formula before any of the compounds can be "at once envisaged." One may look to the preferred embodiments to determine which compounds can be anticipated.” In re Petering, 301 F.2d 676, 133 USPQ 275 (CCPA 1962). Here, although Itagaki et al. exemplifies a hydrophobic peptide where m is 5, given the finite number of hydrophobic peptide species taught by Itagaki, i.e., where m is 5-7 (i.e., Itagaki’s n is 6-8 thereby correlating to instant m being 5-7), an ordinary skilled artisan can at one envisage where instant “m” is 6-7. Thus, Itagaki’s disclosure satisfies the claim limitations as recited in instant claims 4-5.
For claim 6, as discussed supra, Itagaki et al. teaches that poly(sarcosine)-b-(L-Leu-Aib)6 self-assembled into curved sheets just after injection into water, which converted to nanotubes upon heating at 90 °C (See Itagaki, pg. 842, col. 1, 1st paragraph; pg. 844, col. 1, 2nd paragraph). The adenine nanotubes had lengths much longer than the glycolic acid nanotubes, accompanied by bundles and aggregations of the nanotubes (See Itagaki, pg. 844, col. 1, 2nd paragraph). Table 1 also states that the hydrophobic peptide is helical (See Itagaki, pg. 843, Table 1). As such, the hydrophobic peptide forms a rod-shaped alpha-helical structure.
However, it is unnecessary for Itagaki et al. to teach these properties given that Itagaki et al. discloses a specific species of peptide having the claimed structure of General formula I. Therefore, the physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of new physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) which are inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Thus, Itagaki’s disclosure satisfies the claim limitations as recited in instant claim 6.
For claim 7, Itagaki et al. does not expressly disclose that the peptide is controlled to be arranged and oriented in the direction of an external magnetic field. However, it is unnecessary for a prior art reference to teach this limitation because an intended use of the peptide (i.e., being controlled to be arranged and oriented in the direction of an external magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the peptide being controlled to be arranged and oriented in the direction of an external magnetic field is an intended use of the claimed peptide that gives little meaning and purpose to the structure of the claimed peptide. In other words, the claim is directed to the structure of a peptide and not a device or substrate surface that includes the structure of a magnetic field. Accordingly, claim 7 recites an intended use that does not render material to patentability.
For claim 15, Itagaki et al. does not expressly disclose that the peptide complex self-assembles into a spherical nanoparticle such as a vesicular structure in solution. However, it is unnecessary for a prior art reference to teach this limitation because a physical/structural property of the peptide (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, given that Ueda et al. discloses specific species of peptides having the claimed structure of General formula I complexed with a hydrophilic polymer, the physical/structural property of the peptide complex (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) is an intended result of the claimed peptide complex that gives little meaning and purpose to the structure of the claimed peptide. Accordingly, claim 15 recites an intended result that does not render material to patentability.
For claim 20, as discussed supra, Itagaki et al. teaches that poly(sarcosine)-b-(L-Leu-Aib)6 self-assembled into curved sheets just after injection into water, which converted to nanotubes upon heating at 90 °C (See Itagaki, pg. 842, col. 1, 1st paragraph; pg. 844, col. 1, 2nd paragraph). The adenine nanotubes had lengths much longer than the glycolic acid nanotubes, accompanied by bundles and aggregations of the nanotubes (See Itagaki, pg. 844, col. 1, 2nd paragraph). Table 1 also states that the hydrophobic peptide is helical (See Itagaki, pg. 843, Table 1). Although Itagaki et al. does not refer to the structure as a nanoribbon structure, the nanotube structure is formed through self-assembly. It is further noted that Itagaki et al. does not expressly teach that when the peptide complex binds to the nucleic acid material a nanostructure with an artificial chromosome-like structure is formed through self-assembly as the nanoribbon is folded and stacked. The process of self-assembling into a nanostructure constitutes a product-by-process. Regarding product-by-process claims, the Federal Circuit has found that "[e]ven through product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim in the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." See MPEP 2113 and In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). Furthermore, the Federal Circuit found that “[b]ecause validity is determined based on the requirements of patentability, a patent is invalid if a product made by the process recited in a product-by-process claim is anticipated by or obvious from prior art products, even if those prior art products are made by different processes.” See MPEP 2113 and Amgen, Inc. v. F. Hoffman-La Roche Ltd., 580 F.3d 1340, 1370 n 14, 92 USPQ2d 1289, 1312, n 14 (Fed. Cir. 2009). Here, since Itagaki et al. discloses a specific species of composition having the claimed peptide complex structure of claim 18, it would necessarily follow that the peptide complex would self-assemble into a nanostructure with an artificial chromosome-like structure when bound to the adenine. Thus, Itagaki’s disclosure satisfies the claim limitations as recited in instant claim 20.
For claims 22-23, Itagaki et al. does not expressly disclose that the composition nanostructure is degraded at a magnetic field intensity of 0.1-2 T and induces the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field. However, it is unnecessary for a prior art reference to teach these limitations because an intended use of the composition nanostructure (i.e., being degraded at a magnetic field intensity of 0.1-2 T thereby inducing the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed composition. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the composition being degraded at a magnetic field intensity of 0.1-2 T thereby inducing the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field is an intended use of the claimed composition that gives little meaning and purpose to the structure of the claimed composition. In other words, the claim is directed to the structure of a composition, and not a device or substrate surface or a method of using the composition that includes the structure or use of a magnetic field. Accordingly, claims 22-23 recite an intended use that does not render material to patentability.
Accordingly, Itagaki’s disclosure anticipates instant claims 1-8, 15, 18, 20, and 22-23.
Claims 1-3, 6-9, and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rahman et al., Biomacromolecules 20:3908-3914 (2019).
For claims 1-3 and 8-9, Rahman et al. discloses a tubular network that was formed by co-assembling two different amphiphilic polypeptides, poly(ethylene glycol)-b-(L-Leu-Aib)6 (PL12) and polysarcosine-b-(L-Leu-Aib)6 (SL12) (Rahman, abstract). They both have the same hydrophobic 12-mer helical block (L-Leu-Aib)6 but different hydrophilic chains, poly(ethylene glycol) and polysarcosine (Rahman, abstract). In water, both polypeptides self-assembled into a tubular structure having a uniform 80 nm diameter that was formed by packing among the hydrophobic L12 blocks (Rahman, abstract). The SL12 nanotubes were short (200 nm), straight, and robust. PL12 formed long (>1 μm), bendable, and fusogenic nanotubes (Rahman, abstract). The structures of the amphiphilic polypeptides are:
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(See Rahman, Figure 1B). The peptide component, i.e., (L-Leu-Aib)6 would correlate to a peptide with the general formula of L-Leu-(Aib-L-Leu)5-Aib where the C-terminus is modified with -OCH3 and the N-terminus is complexed with poly(sarcosine) or PEG, each of which constitute a hydrophilic polymer.
With respect to the peptide being hydrophobic, Rahman et al. expressly teaches that the (L-Leu-Aib)6 portion of the amphiphilic peptide is hydrophobic in nature, i.e., hydrophobic helical block (See Rahman, pg. 3908, col. 1, last paragraph). However, the physical property (i.e., being hydrophobic) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new physical property (i.e., being hydrophobic) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977).
Thus, the specific species disclosed by Rahman et al. constitutes a hydrophobic peptide represented by instant General Formula I where Xaa1 is L-Leu and m is 5 as recited in instant claims 1-3, a peptide complex comprising the peptide of claim 1 and a hydrophilic polymer bound to one end of the peptide as recited in instant claim 8, and where the hydrophilic polymer is PEG as recited in instant claim 9.
For claim 6, Rahman et al. teaches that both the amphiphilic polypeptides for nanotubes where the polysarcosine polypeptides form rigid nanotubes whereas the PEG polypeptides is more flexible allowing the nanotubes to bend (See Rahman, pg. 3908, col. 1, last paragraph to col. 2, last paragraph). Rahman et al. also refers to the hydrophobic block of the polypeptides as helical (See Rahamn, pg. 3908, col. 1, last paragraph). As such, the hydrophobic peptide forms a rod-shaped alpha-helical structure.
However, it is unnecessary for Rahman et al. to teach these properties given that Rahman et al. discloses specific species of peptides having the claimed structure of General formula I. Therefore, the physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of new physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) which are inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Thus, Rahman’s disclosure satisfies the claim limitations as recited in instant claim 6.
For claim 7, Rahman et al. does not expressly disclose that the peptide is controlled to be arranged and oriented in the direction of an external magnetic field. However, it is unnecessary for a prior art reference to teach this limitation because an intended use of the peptide (i.e., being controlled to be arranged and oriented in the direction of an external magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the peptide being controlled to be arranged and oriented in the direction of an external magnetic field is an intended use of the claimed peptide that gives little meaning and purpose to the structure of the claimed peptide. In other words, the claim is directed to the structure of a peptide and not a device or substrate surface that includes the structure of a magnetic field. Accordingly, claim 7 recites an intended use that does not render material to patentability.
For claim 15, Rahman et al. does not expressly disclose that the peptide complex self-assembles into a spherical nanoparticle such as a vesicular structure in solution. However, it is unnecessary for a prior art reference to teach this limitation because a physical/structural property of the peptide (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, given that Ueda et al. discloses specific species of peptides having the claimed structure of General formula I complexed with a hydrophilic polymer, the physical/structural property of the peptide complex (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) is an intended result of the claimed peptide complex that gives little meaning and purpose to the structure of the claimed peptide. Accordingly, claim 15 recites an intended result that does not render material to patentability.
Accordingly, Rahman’s disclosure anticipates instant claims 1-3, 6-9, and 15.
Claims 1-3, 6-8, and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Ueda et al., Chem. Commun. 47:3204-3206 (2011).
For claims 1-3 and 8, Ueda et al. discloses amphiphilic peptide nanotubes with the structures:
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(See Ueda, pg. 3204, col. 1). When the right-handed helix is mixed with the left-handed helix, they are expected to form a stereo-complex probably due to the convexo-concave fitness between their surfaces (See Ueda, pg. 3204, col. 1, 1st paragraph). By using stereo-complex formation of these helical peptides, Ueda et al. demonstrate vesicle formation from two types of peptide nanotubes by membrane fusion (See Ueda, pg. 3204, col. 1, 1st paragraph). As such, the peptide component, i.e., (L-Leu-Aib)6 or (D-Leu-Aib)6, would correlate to a peptide with the general formula of L-Leu-(Aib-L-Leu)5-Aib and D-Leu-(Aib-D-Leu)5-Aib, respectively, where the C-terminus is modified with -OCH3 and the N-terminus is complexed with poly(sarcosine), which constitutes a hydrophilic polymer.
With respect to the peptide being hydrophobic, Ueda et al. expressly teaches that the (L-Leu-Aib)6 or (D-Leu-Aib)6 portion of the amphiphilic peptide is hydrophobic in nature, i.e., hydrophobic helical block (See Rahman, pg. 3908, col. 1, last paragraph). However, the physical property (i.e., being hydrophobic) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new physical property (i.e., being hydrophobic) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977).
Thus, the specific species disclosed by Ueda et al. constitutes a hydrophobic peptide represented by instant General Formula I where Xaa1 is L-Leu and m is 5 as recited in instant claims 1-3, and a peptide complex comprising the peptide of claim 1 and a hydrophilic polymer bound to one end of the peptide as recited in instant claim 8.
For claim 6, Ueda et al. teaches that the SLL (i.e., hydrophobic peptide containing L-Leu) self-assembles into a homogeneous nano curved-sheet morphology (See Ueda, pg. 3204, col. 2, last paragraph) thereby constituting a rod-shaped hydrophobic peptide. Moreover, Ueda et al. refers to the hydrophobic portion of the amphiphilic peptide as a hydrophobic helical peptide (See Ueda, pg. 3204, col. 1, last paragraph) thereby constituting where the hydrophobic peptide has an alpha-helical structure.
However, it is unnecessary for Ueda et al. to teach these properties given that Ueda et al. discloses specific species of peptides having the claimed structure of General formula I. Therefore, the physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) of the peptide as claimed and the known peptide are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of new physical/structural properties (i.e., being rod-shaped and having an alpha-helix structure) which are inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Thus, Ueda’s disclosure satisfies the claim limitations as recited in instant claim 6.
For claim 7, Ueda et al. does not expressly disclose that the peptide is controlled to be arranged and oriented in the direction of an external magnetic field. However, it is unnecessary for a prior art reference to teach this limitation because an intended use of the peptide (i.e., being controlled to be arranged and oriented in the direction of an external magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the peptide being controlled to be arranged and oriented in the direction of an external magnetic field is an intended use of the claimed peptide that gives little meaning and purpose to the structure of the claimed peptide. In other words, the claim is directed to the structure of a peptide and not a device or substrate surface that includes the structure of a magnetic field. Accordingly, claim 7 recites an intended use that does not render material to patentability.
For claim 15, as discussed supra, Ueda et al. discloses that when the right-handed helix is mixed with the left-handed helix, they are expected to form a stereo-complex probably due to the convexo-concave fitness between their surfaces (See Ueda, pg. 3204, col. 1, 1st paragraph). By using stereo-complex formation of these helical peptides, Ueda et al. demonstrate vesicle formation from two types of peptide nanotubes by membrane fusion (See Ueda, pg. 3204, col. 1, 1st paragraph; pg. 3205, col. 1, 2nd paragraph). As such, when combining both amphiphilic peptides at an equimolar ratio, the initial planar square sheets are transformed into vesicles (See Ueda, pg. 3205, col. 1, 2nd paragraph). Ueda et al. demonstrate a new method for vesicle formation by a novel fusion mechanism that is driven by the stereo-complex formation of the helical amphiphiles (See Ueda, pg. 3206, col. 1, last paragraph). The morphology transformation process from the nanotube to the vesicle is composed of four steps: (i) nanotube association, (ii) mixing of right- and left-handed helices, (iii) break-up of the tubular structure to the planar sheet structure, and (iv) closing to the vesicular structure (See Ueda, pg. 3206, col. 1, last paragraph to col. 2, 1st paragraph).
However, it is unnecessary for a prior art reference to teach this limitation because a physical/structural property of the peptide (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed peptide. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, given that Ueda et al. discloses specific species of peptides having the claimed structure of General formula I complexed with a hydrophilic polymer, the physical/structural property of the peptide complex (i.e., self-assembles into a spherical nanoparticle such as a vesicular structure in solution) is an intended result of the claimed peptide complex that gives little meaning and purpose to the structure of the claimed peptide. Accordingly, claim 15 recites an intended result that does not render material to patentability.
Accordingly, Ueda’s disclosure anticipates instant claims 1-3, 6-8, and 15.
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.
is
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under pre-AIA 35 U.S.C. 103(a) are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims under 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of 35 U.S.C. 103(c) and potential 35 U.S.C. 102(e), (f) or (g) prior art under 35 U.S.C. 103(a).
103 - KSR Examples of 'Rationales' Supporting a Conclusion of Obviousness(Consistent with the "Functional Approach" of Graham)
Further regarding 35 USC 103(a) rejections, the Supreme Court in KSR International Co. v. Teleflex Inc., 550 U.S. 398, 127 S. Ct. 1727, 82 USPQ2d 1385, 1395-97 (2007) (KSR) identified a number of rationales to support a conclusion of obviousness which are consistent with the proper "functional approach" to the determination of obviousness as laid down in Graham. The key to supporting any rejection under 35 U.S.C. 103 is the clear articulation of the reason(s) why the claimed invention would have been obvious. The Supreme Court in KSR noted that the analysis supporting a rejection under 35 U.S.C. 103 should be made explicit.
Exemplary rationales that may support a conclusion of obviousness include:
(A) Combining prior art elements according to known methods to yield predictable results;
(B) Simple substitution of one known element for another to obtain predictable results;
(C) Use of known technique to improve similar devices (methods, or products) in the same way;
(D) Applying a known technique to a known device (method, or product) ready for improvement to yield predictable results;
(E) "Obvious to try" - choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success;
(F) Known work in one field of endeavor may prompt variations of it for use in either the same field or a different one based on design incentives or other market forces if the variations are predictable to one of ordinary skill in the art;
(G) Some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention.
Note that the list of rationales provided is not intended to be an all-inclusive list. Other rationales to support a conclusion of obviousness may be relied upon by Office personnel.
Also, a reference is good not only for what it teaches by direct anticipation but also for what one of ordinary skill in the art might reasonably infer from the teachings. (In re Opprecht 12 USPQ 2d 1235, 1236 (Fed Cir. 1989); In re Bode 193 USPQ 12 (CCPA) 1976).
Claims 8-9, 13, 15, and 18-23 are rejected under 35 U.S.C. 103 as being unpatentable over Ueda et al., Chem. Commun. 47:3204-3206 (2011), as applied to claims 8-9 and 15 above, and further in view of Yang et al. US 2010/0286069 A1 published on November 11, 2010, as applied to claims 13, 18-19 and 21-23.
For claims 8-9, 13, 18-19, and 21, as discussed supra, Ueda et al. teaches amphiphilic peptide nanotubes with the structures:
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(See Ueda, pg. 3204, col. 1). When the right-handed helix is mixed with the left-handed helix, they are expected to form a stereo-complex probably due to the convexo-concave fitness between their surfaces (See Ueda, pg. 3204, col. 1, 1st paragraph). By using stereo-complex formation of these helical peptides, Ueda et al. demonstrate vesicle formation from two types of peptide nanotubes by membrane fusion (See Ueda, pg. 3204, col. 1, 1st paragraph). Ueda et al. demonstrate a new method for vesicle formation by a novel fusion mechanism that is driven by the stereo-complex formation of the helical amphiphiles (See Ueda, pg. 3206, col. 1, last paragraph). The morphology transformation process from the nanotube to the vesicle is composed of four steps: (i) nanotube association, (ii) mixing of right- and left-handed helices, (iii) break-up of the tubular structure to the planar sheet structure, and (iv) closing to the vesicular structure (See Ueda, pg. 3206, col. 1, last paragraph to col. 2, 1st paragraph). Thus, the specific species disclosed by Ueda et al. constitutes a hydrophobic peptide represented by instant General Formula I where Xaa1 is L-Leu and m is 5 as recited in instant claims 1-3, a peptide complex comprising the peptide of claim 1 and a hydrophilic polymer bound to one end of the peptide as recited in instant claim 8, and where the hydrophilic polymer is PEG as recited in instant claim 9.
However, Ueda et al. does not expressly teach where the amphiphilic polypeptides that form a vesicle can form a non-covalent bond with DNA thereby forming a composition as recited in instant claims 18-19 and 21, or where the amphiphilic polypeptides contain 1-4 positively charged amino acids at the N- or C-terminus of the peptide complex as recited in instant claim 13.
Yang et al. teaches a triblock peptide comprising a hydrophobic amino acid block, a histidine block, and a cationic amino acid block that forms a nanoparticle for delivery of an agent such as nucleic acids, e.g., DNA or RNA, into a cell (See Yang, abstract; [0008], [0010], [0041], [0047], [0075]). The hydrophobic block is included to allow for cell membrane penetration by the peptide and any agent including a nucleic acid molecule, which can be complexed with the peptide (See Yang, [0043]). The hydrophobic block also provides a self-assembling core portion that promotes formation of the core-shell nanoparticles and which can serve to encapsulate agents that are hydrophobic (See Yang, [0043]).
The cationic block provides positive charges that allow for efficient binding of nucleic acid molecules or other agent that may be negatively charged or have a negatively charged surface or region (See Yang, [0042]). The cationic block can be composed of a single type of cationic amino acid, for example, all arginine residues (See Yang, [0059]). The length of the cationic amino acid block can vary, and can be 5 to 25 hydrophilic residues, e.g., 5 arginine residues (See Yang, [0061], [0063]). Thus, the negative charges on the agent allow the agent to form a complex with the cationic nanoparticle via electrostatic interaction (See Yang, [0081]) thereby constituting where the peptide complex and the nucleic acid are noncovalently bound.
With respect to where the peptide complex further comprises a positively charged peptide consisting of 4 positively charged residues at the N- or C-terminal of the complex where the positively charged residues are arginine, although Yang et al. teaches utilizing a minimum of 5 positively charged amino acid residues instead of 4, an ordinary skilled artisan would expect that 4 positively charged arginine residues would exhibit similar properties to Yang’s 5 arginine residues by allowing for efficient binding of nucleic acid molecules that are negatively charged. Pursuant to MPEP 2144.09(I), [a] prima facie case of obviousness may be made when chemical compounds have very close structural similarities and similar utilities. "An obviousness rejection based on similarity in chemical structure and function entails the motivation of one skilled in the art to make a claimed compound, in the expectation that compounds similar in structure will have similar properties." In re Payne, 606 F.2d 303, 313, 203 USPQ 245, 254 (CCPA 1979). See In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA 1963) and In re Dillon, 919 F.2d 688, 16 USPQ2d 1897 (Fed. Cir. 1990).
Additionally and/or alternatively, a prima facie case of obviousness exists where the claimed ranges and prior art ranges do not overlap but are close enough that one skilled in the art would have expected them to have the same properties. Titanium Metal Corp. of America v. Banner, 778 F.2d 775, 227 USPQ 773 (Fed. Cir. 1985) (Court held a proper rejection of a claim directed toward an alloy of having "0.8% nickel, 0.3% molybdenum, 0.1% iron, balance titanium" as obvious over a reference disclosing alloys of 0.75% nickel, 0.25% molybdenum, balance titanium and 0.94% nickel, 0.31% molybdenum, balance titanium.) Therefore, the claimed number of arginine residues would have been suggested to one skilled in the art because the claimed number of arginine residues (i.e., 1-4 arginine residues) is close to the taught number of arginine residues (i.e., 5-25).
With respect to where the peptide complex and the nucleic acid material self-assemble into a nanostructure having an artificial chromosome-like structure via noncovalent bonding, although the combination of Ueda and Yang do not refer to the structure as a nanoribbon structure, the nanotube structure is formed through self-assembly. It is further noted that the combination of Ueda and Yang do not expressly teach that when the peptide complex binds to the nucleic acid material a nanostructure with an artificial chromosome-like structure is formed through self-assembly via noncovalent bonding. The process of self-assembling into a nanostructure constitutes a product-by-process. Regarding product-by-process claims, the Federal Circuit has found that "[e]ven through product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim in the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." See MPEP 2113 and In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). Furthermore, the Federal Circuit found that “[b]ecause validity is determined based on the requirements of patentability, a patent is invalid if a product made by the process recited in a product-by-process claim is anticipated by or obvious from prior art products, even if those prior art products are made by different processes.” See MPEP 2113 and Amgen, Inc. v. F. Hoffman-La Roche Ltd., 580 F.3d 1340, 1370 n 14, 92 USPQ2d 1289, 1312, n 14 (Fed. Cir. 2009). Here, since the combination of Ueda and Yang suggests the noncovalent binding of Ueda’s peptide complex modified with 4 arginine residues at the N- or C-terminus to DNA or RNA thereby constituting the composition of instant claim 18, it would necessarily follow that the composition would self-assemble into a nanostructure with an artificial chromosome-like structure, especially since the structural requirement of noncovalent bonding is present.
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the instant application to modify the teachings of Ueda et al. and fuse 4 arginine residues to the N- or C-terminus of Ueda’s SLL and SDL thereby allowing for noncovalent binding to negatively charged DNA or RNA in order to form a vesicular nanoparticle such that the SLL and SDL delivers the DNA or RNA into a cell. One of ordinary skill in the art at the time the invention was made would have been motivated to do so because a triblock peptide comprising a hydrophobic amino acid block, a histidine block, and a cationic amino acid block containing 5-25 arginine residues was known to form a nanoparticle for delivery of an agent such as nucleic acids, e.g., DNA or RNA, into a cell via noncovalently binding between the cationic arginine residues of the peptide complex and the negatively charged DNA or RNA as taught by Yang e al. One of ordinary skill in the art at the time the invention was made would have had a reasonable expectation of success given that the peptide complex of Ueda et al. contained a mixture of amphiphilic peptides comprising a hydrophobic helical block of (L/D-Leu-Aib) and a hydrophilic polymer of poly(Sar) or PEG where such mixture formed a vesicular nanoparticle structure. Therefore, modifying the peptide complex of Ueda by fusing 4 arginine residues at the N- or C-terminus of the complex thereby allowing for the noncovalent binding of the arginine residues to negatively charged DNA or RNA would support the delivery of the DNA or RNA into a cell by constituting some teaching, suggestion, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the claimed invention pursuant to KSR.
For claim 15, please see discussion of Ueda et al. supra in the 102(a)(1) rejection.
For claim 20, although the combination of Ueda and Yang do not refer to the structure as a nanoribbon structure, the nanotube structure is formed through self-assembly. It is further noted that the combination of Ueda and Yang do not expressly teach that when the peptide complex binds to the nucleic acid material a nanostructure with an artificial chromosome-like structure is formed through self-assembly as the nanoribbon is folded and stacked. The process of self-assembling into a nanostructure constitutes a product-by-process. Regarding product-by-process claims, the Federal Circuit has found that "[e]ven through product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim in the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." See MPEP 2113 and In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). Furthermore, the Federal Circuit found that “[b]ecause validity is determined based on the requirements of patentability, a patent is invalid if a product made by the process recited in a product-by-process claim is anticipated by or obvious from prior art products, even if those prior art products are made by different processes.” See MPEP 2113 and Amgen, Inc. v. F. Hoffman-La Roche Ltd., 580 F.3d 1340, 1370 n 14, 92 USPQ2d 1289, 1312, n 14 (Fed. Cir. 2009). Here, since the combination of Ueda and Yang suggests the noncovalent binding of Ueda’s peptide complex modified with 4 arginine residues at the N- or C-terminus to DNA or RNA thereby constituting the composition of instant claim 18, it would necessarily follow that the composition would self-assemble into a nanostructure with an artificial chromosome-like structure where the nanoribbon is folded and stacked, especially since the structural requirement of noncovalent bonding is present. Therefore, the limitations of claim 20 are necessarily met in light of the combination of Ueda and Yang.
For claims 22-23, the combination of Ueda and Yang do not expressly teach that the composition nanostructure is degraded at a magnetic field intensity of 0.1-2 T and induces the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field. However, it is unnecessary for a prior art reference to teach these limitations because an intended use of the composition nanostructure (i.e., being degraded at a magnetic field intensity of 0.1-2 T thereby inducing the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field) does not state a condition that is material to patentability or provide a structural limitation that would further limit the claimed composition. The court has found that the determination of whether clauses such as “wherein” and “whereby" is a limitation in a claim is dependent on the specific facts of the case. If the “wherein" or “whereby” clause limits a process claim where the clause gives meaning and purpose to the manipulative steps, it should be given patentable weight. However, the court also found (quoting Minton v. Nat’l Ass’n of Securities Dealers, Inc., 336 F.3d 1373, 1381, 67 USPQ2d 1614, 1620 (Fed. Cir. 2003)) that a “‘whereby clause in a method claim is not given weight when it simply expresses the intended result of a process step positively recited.’” In the instant case, the composition being degraded at a magnetic field intensity of 0.1-2 T thereby inducing the release of the nucleic acid material where the magnetic field intensity is 0.1-0.5 T based on a rotating magnetic field is an intended use of the claimed composition that gives little meaning and purpose to the structure of the claimed composition. In other words, the claim is directed to the structure of a composition, and not a device or substrate surface or a method of using the composition that includes the structure or use of a magnetic field. Accordingly, claims 22-23 recite an intended use that does not render material to patentability.
Thus, the invention as a whole is prima facie obvious over the references, especially in the absence of evidence to the contrary.
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 1-9, 13, 15, and 18-23 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11-13 and 15-31 of copending Application No. 18/185,167 (US 2024/0116986 A1). Although the claims at issue are not identical, they are not patentably distinct from each other because ‘167 claims:
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(See ‘167, claims 11-12, 15-17, and 20-24). As such, ‘167’s fusion peptide constitutes the instant hydrophobic peptide, i.e., ‘167 SEQ ID NOs: 4-8, where Xaa1 is L-Ala and m is 4-6, the instant positively charged peptide consisting of 1-4 positively charged amino acids at the N- or C-terminal of the hydrophobic peptide, i.e., ‘167’s gene-binding region, and the instant peptide complex comprising a hydrophilic polymer where the hydrophilic polymer is PEG as recited in instant claims 1-5, 8-9, and 13. ‘167’s peptide-molecule conjugate forming a self-assembled monolayer that surrounds a nucleic acid material such as DNA or RNA through non-covalent binding further constitutes the instant composition where the nucleic acid material is DNA or RNA as recited in instant claims 18 and 21. Thus, the ‘167 claimed invention anticipates the instantly claimed structures as recited in instant claims 1-5, 8-9, 13, 18, and 21.
With respect to the hydrophobic peptide being rod-shaped and having an alpha-helix structure, ‘167 claims the peptide-molecule conjugate has a helicity of 0.8-0.9 (See ‘167, claim 13) and is in the shape of a nanotube (See ‘167, claim 21) thereby satisfying instant claim 6.
With respect to where the peptide complex self-assembles into a spherical nanoparticle such as a vesicular structure in solution, ‘167 claims where the peptide-molecule conjugate forming a self-assembled monolayer that surrounds a nucleic acid material such as DNA or RNA through non-covalent binding (See ‘167 claims 15 and 20) thereby constituting a spherical nanoparticle structure such a vesicle structure thereby satisfying instant claim 15.
With respect to instant claims 7, 19-20, and 22-23, although ‘167 does not expressly claim these intended uses and/or physical/structural properties, since ‘167 claims the hydrophobic peptide of instant claim 1, the peptide complex of instant claim 8, and the composition of instant claim 18, the ‘167 claimed invention would be capable of performing the claimed intended uses and/or necessarily exhibit the physical/structural properties. Properties are the same when the structure and composition are the same. Thus, burden shifts to applicant to show unexpected results, by declaration or otherwise. In re Fitzgerald, 205 USPQ 594. In the alternative, the claimed properties would have been present once the composition was employed in its intended use. In re Best, 195 USPQ 433.
Thus, the ‘167 claimed invention is not patentably distinct from the instantly claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to THEA D' AMBROSIO whose telephone number is (571)270-1216. The examiner can normally be reached M-F 11:00 to 8:00 pm.
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/THEA D' AMBROSIO/Primary Examiner, Art Unit 1654
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