DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1 and 3-12 drawn to a method for treating comprising administering to a patient in need thereof an effective amount of serum albumin nanoparticles (Alb-NP) decorated with at least one decoration chain comprising a linker, bound to the nanoparticles by means of an -S- thioether bond, and at least one biological molecule, and species comprising the following:
PNG
media_image1.png
143
440
media_image1.png
Greyscale
in the reply filed on 4/20/2026 is acknowledged.
Claims 1-22 are pending in the instant application.
Claims 2, 11, and 13-22 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 4/20/2026.
Claims 1, 3-10, and 12 are being examined on the merit.
In regards to instant claim 11, although it was grouped under Group I, instant claim 11 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim.
Applicant is reminded that upon the cancelation of claims to a non-elected invention, the inventorship must be corrected in compliance with 37 CFR 1.48(a) if one or more of the currently named inventors is no longer an inventor of at least one claim remaining in the application. A request to correct inventorship under 37 CFR 1.48(a) must be accompanied by an application data sheet in accordance with 37 CFR 1.76 that identifies each inventor by his or her legal name and by the processing fee required under 37 CFR 1.17(i).
Information Disclosure Statement
Applicant’s IDS submitted 5/26/2023 has been acknowledged and considered. Signed copies are attached hereto.
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 - This application fails to comply with the requirements of 37 CFR 1.831-1.834 because it does not contain a “Sequence Listing XML” as a separate part of the disclosure. A “Sequence Listing XML” is required because the instant application contains amino acid sequences of 4 amino acids or more that requires an appropriate Sequence Listing XML and SEQ ID NOs for the corresponding amino acid sequences.
Required response - Applicant must provide:
• A “Sequence Listing XML” part of the disclosure, as described above in item 1. or 2.; together with
o A statement that indicates the basis for the amendment, with specific references to particular parts of the application as originally filed, as required by 37 CFR 1.835(a)(3);
o A statement that the “Sequence Listing XML” includes no new matter as required by 37 CFR 1.835(a)(4)
AND
• A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required incorporation by reference paragraph as required by 37 CFR 1.835(a)(2), consisting of:
o A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
o A copy of the amended specification without markings (clean version); and
o A statement that the substitute specification contains no new matter.
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). Amino acid sequences of 4 or more amino acids require a sequence identifier. Claim 10 and pages 9, 18, 20-23, 25-26, and 29-32 of the instant specification do not include SEQ ID NOs for the amino acid sequences. Amendment to the claim and specification to include SEQ ID NOs for the amino acid sequences are required.
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.
Specification
The disclosure is objected to because of the following informalities: pages 9, 18, 20-23, 25-26, and 29-32 of the instant specification do not include SEQ ID NOs for the amino acid sequences.
Appropriate correction is required.
Claim Objections
Claim 10 is objected to because of the following informalities: the amino acid sequences comprised of 4 amino acids that describe the consensus sequence comprising the albumin nanoparticle are missing sequence identifiers (SEQ ID NO:XX). Appropriate correction is required.
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.
Claims 1, 3-10, and 12 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.
Claims 1, 4, 5, and 6 recite exemplary language that renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. Specifically, the phrase “preferably” renders the claim indefinite in regards to instant claims 1, 4, 5, and 6 because it is unclear whether the limitations following the phrase are part of the claimed invention.
Claim 4 further recites exemplary language that renders the claim indefinite because it is unclear whether the limitation is part of the claimed invention. Specifically, the limitation in the parenthesis renders the claim indefinite in regards to instant claim 4, because it is unclear whether the limitation in the parenthesis is part of the claimed invention.
Claim 6 contains the trademark/trade name nanobodies (Nanobody®). Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe the biological molecule comprising the Alb-NP used in the method for treating a pathology, e.g. breast cancer, and, accordingly, the identification/description is indefinite.
Claim Rejections - 35 USC § 103
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 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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1, 3-4, 7-10, and 12 are rejected under 35 U.S.C. 103 as being unpatentable over Selis et al (International Journal of Biological Macromolecules, epub available on 9/14/2020, 164:4516-4531, IDS entered on 5/2/2023; hereinafter Selis), and further in view of Ehrlich et al (Bioconjugate Chemistry, 2013, 24(12): 2015-2024; hereinafter Ehrlich), and Yurkovetskiy et al (WO2014/093379 A1; hereinafter, Yurkovetskiy).
Regarding claims 1, 3-4, 7-10, and 12, Selis discloses recombinant antibodies to use in diagnostic and therapeutic applications as anti-cancer molecules (page 2015, Abstract; Fig. 8). Selis teaches a trastuzumab (an anti-Her2 monoclonal antibody currently used for treating human breast cancers) Fab variant (Trast-rFab-TQGA), wherein the variant bears a consensus motif (TQGA) sensitive to MTG modifications to enable efficient site specific and covalent functionalization and to generate molecules that are active at least as the related full-length antibody (page 4517, left column, last paragraph – right column, paragraph 1). Selis additionally teaches Trast-rFab-TQGA conjugated to the lysine residue of the peptide linker containing the amino acid sequence KAYA (L-Lys-L-Ala-L-Tyr-L-Ala), an MTG amine substrate, through reactions mediated by MTG (page 4519, right column, section 2.5.1; page 4519, left column, section 2.4; and Scheme 1A). Selis further discloses that the use of transamidation with transglutaminase (MTG) for linking antibody fragments is known (page 4529, right column, second paragraph).
However, Selis does not teach coupling of the antibody (biological molecule) to human albumin nanoparticles comprising a linker, wherein the linker is bound to the nanoparticle by means of an -S- thioether bond and the linker comprises Z-spacer wherein (i) Z derives from a functional group containing an electrophile group capable of reacting with the -SH group of the albumin, thereby forming the -S-thioether bond, wherein the functional group is from 6-maleimidohexanoic acid; and (ii) the spacer is glycine. Selis also does not teach the nanoparticles having an average diameter (or Z-average size) of 100-500 nm measured with the Dynamic Light Scattering (DLS) technique
The deficiency is resolved by Ehrlich and Yurkovetskiy.
Ehrlich teaches the conjugation of recombinant HSA to a peptide analogue using heterobifunctional linkers, one of which was 6-maleimidohexanoic acid N-hydroxysuccinimide ester (MHS), wherein proteolytic digests of the conjugate revealed that peptide conjugation occurred at the Cys34 residue on HSA (page 2015, Abstract). Ehrlich also teaches that HSA not only has a circulation half-life of 21 days in humans, but also at the molecular level, HSA has a free cysteine (Cys34), which makes it an ideal molecule for site-specific conjugation (page 2016, left column, second and third paragraphs). Furthermore, Ehrlich discloses that the albumin conjugates generated using MHS (HSA-MH-Y2R) displayed greater biological effect in vivo (page 2020, left column, second and third paragraphs; Figures 7 and 8; Table 4).
Yurkovetskiy teaches pharmaceutically acceptable formulations comprising nanoparticles comprising auristatin compound conjugates, wherein the auristatin compound conjugate comprises a protein-based recognition molecule, a stretcher unit, a drug moiety comprised of a polymeric carrier linked to a drug compound auristatin, and a spacer unit that links the stretcher unit to the drug moiety. Yurkovetskiy further teaches that a glycine spacer unit was used, wherein when an exemplary compound containing the glycine spacer unit undergoes enzymatic cleavage via a tumor-cell associated-protease, a cancer-cell-associated protease or a lymphocyte-associated protease, a hydrolysis reaction takes place within the target cell, cleaving the glycine-Drug moiety bond and liberating the Drug (page 125, paragraphs [00410]-[00411], “The Spacer Unit” section; pages 173-174, paragraph [00569]).
Regarding instant claims 1,3, 7-10, and 12, it would have been obvious for a person having ordinary skill in the art at the time of filing to modify the recombinant antibody comprising the Fab of trastuzumab, an antibody used to treat human breast cancer, Trast-rFab-TQGA, conjugated to the L-lysine residue of a peptide linker of Selis to further comprise a glycine spacer unit of Yurkovetskiy and a functional group 6-maleimidohexanoic acid conjugated to HSA as taught by Ehrlich. This is obvious because, Selis discloses Trast-rFab-TQGA, a recombinant antibody for use in diagnostic and therapeutic applications as an anti-cancer molecule, wherein the variant bears a consensus motif (TQGA) sensitive to MTG modifications conjugated to a L-lysine residue of a peptide linker through reactions mediated by MTG, Yurkovetskiy teaches that a glycine spacer unit is used for liberation of a drug moiety in the target cell through an enzymatic cleavage via a tumor-cell associated-protease, and Ehrlich teaches the conjugation of recombinant HSA to a peptide analogue at the Cys34 residue on HSA using heterobifunctional linkers, such as 6-maleimidohexanoic acid N-hydroxysuccinimide ester (MHS), because the HSA albumin conjugates generated using MHS displayed greater biological effect in vivo. Therefore, it is obvious to a skilled artisan with reasonable expectation of success to form the instant method for treating breast cancer comprising administering to a patient in need thereof an effective amount of human albumin nanoparticles as shown below in Formula X, comprising a functional group 6-maleimidohexanoic acid, a glycine spacer unit, a consensus motif TQGA conjugated to the peptide linker comprising an L-lysine, and the biological molecule an anti-HER2 Fab.
PNG
media_image2.png
172
532
media_image2.png
Greyscale
Claims 4 is rejected under 35 U.S.C. 103 as being unpatentable over Selis et al (International Journal of Biological Macromolecules, epub available on 9/14/2020, 164:4516-4531, IDS entered on 5/2/2023; hereinafter Selis), Ehrlich et al (Bioconjugate Chemistry, 2013, 24(12): 2015-2024; hereinafter Ehrlich), and Yurkovetskiy et al (WO2014/093379 A1; hereinafter, Yurkovetskiy) as applied to claim 1 above, and further in view of Steinhauser et al (Biomaterials, 2006, 27(28):4975-4983; hereinafter Steinhauser).
Regarding instant claim 4, the combined teachings of Selis, Ehrlich, and Yurkovetskiy are discussed above.
However, the combined teachings of Selis, Ehrlich, and Yurkovetskiy does not teach a method for treating breast cancer comprising administering to a patient in need thereof an effective amount of human albumin nanoparticles as shown below in Formula X above, wherein the nanoparticles have an average diameter of 100-500nm.
The deficiency is resolved by Steinhauser.
Steinhauser teaches the coupling of the antibody trastuzumab covalently attached in its thiolated form to human serum albumin (HSA) nanoparticles to take advantage of the capability of HER2-positive cells to incorporate substances binding to HER2 (page 4975, abstract; page 4977, right column, last paragraph; Fig. 1). Steinhauser further teaches that the thiolated trastuzumab was covalently bound to the nanoparticle by thioether formation (page 4979, left column, first paragraph of section 3.2). Steinhauser also teaches that the trastuzumab-modified HSA nanoparticles were approximately 220.5nm in diameter compared to 210.4nm of control HSA nanoparticles as measured by photon correlation spectroscopy, also known as Dynamic Light Scattering (page 4979, left column, section 3.2; Table 2; Fig.3; page 4977, left column, section 2.5).
Regarding instant claim 4, it would have been obvious for a person having ordinary skill in the art at the time of filing to substitute trastuzumab-modified HSA nanoparticles of Steinhauser with the human albumin nanoparticle of formula X as taught by the combined teachings of Selis, Ehrlich and Yurkovetskiy to have an average diameter of approximately 220.5nm as taught by Steinhauser. This is obvious because, the combined teachings of Selis, Ehrlich and Yurkovetskiy teach the conjugation of HSA to a peptide analogue, wherein the peptide analogue comprises a functional group 6-maleimidohexanoic acid, a glycine spacer unit, a consensus motif TQGA conjugated to the peptide linker comprising an L-lysine, and the biological molecule trastuzumab that can be used for diagnostic and therapeutic applications as an anti-cancer molecule for cancers such as human breast cancer, and Steinhauser teaches the coupling of the antibody trastuzumab covalently attached in its thiolated form to HSA nanoparticles, wherein the trastuzumab-modified HSA nanoparticles were approximately 220.5nm in diameter compared to 210.4nm of control HSA nanoparticles as measured by Dynamic Light Scattering. Therefore, it is obvious to a skilled artisan with reasonable expectation of success to form the instant method for treating breast cancer comprising administering to a patient in need thereof an effective amount of human albumin nanoparticles as shown in Formula X, wherein the nanoparticles have an average diameter of 100-500nm measured with via Dynamic Light Scattering.
Claims 5 and 6 are rejected under 35 U.S.C. 103 as being unpatentable over Selis et al (International Journal of Biological Macromolecules, epub available on 9/14/2020, 164:4516-4531, IDS entered on 5/2/2023; hereinafter Selis), Ehrlich et al (Bioconjugate Chemistry, 2013, 24(12): 2015-2024; hereinafter Ehrlich), and Yurkovetskiy et al (WO2014/093379 A1; hereinafter, Yurkovetskiy) as applied to claim 1 above, and further in view of Scheuer et al (Cancer Res., 2009, 69(24):9330-9336; hereinafter Scheuer).
Regarding instant claims 5 and 6, the combined teachings of Selis, Ehrlich, and Yurkovetskiy are discussed above.
However, the combined teachings of Selis, Ehrlich, and Yurkovetskiy do not teach a method for treating breast cancer comprising administering to a patient in need thereof an effective amount of human albumin nanoparticles as shown in Formula X, wherein the R1 and R2 are two different types of Fab: Fab 1 and Fab 2 comprising Trastuzumab and Pertuzumab.
The deficiency is resolved by Scheuer.
Scheuer teaches that trastuzumab is a humanized monoclonal antibody that binds to the extracellular domain of HER2, inhibiting HER2-mediated proliferation by activating antibody-dependent cellular cytotoxicity (ADCC), preventing formation of p9HER2, blocking ligand-independent HER2 signaling, and inhibiting HER2-mediated angiogenesis (page 9330, right column, second paragraph). Scheuer also teaches that Pertuzumab is a humanized monoclonal antibody, wherein Pertuzumab is the first in a new class of HER2 dimerization inhibitors that block HER2 dimerization with other HER family members, such as HER1 or HER3, thus inhibiting the downstream signaling processes that are associated with tumor growth and progression (page 9330, Abstract, page 9330, right column, third paragraph). Scheuer further teaches that the differing mechanisms of action of trastuzumab and pertuzumab can act in a complementary fashion to provide a more complete blockade of HER2-mediated signal transduction than either agent alone (page 9335, right column, third paragraph). In this context, Scheuer discloses that while monotherapy with either trastuzumab or pertuzumab has moderate growth inhibitory effect on NSCLC and breast xenograft tumors, the combination treatment with trastuzumab and pertuzumab induced a strongly enhanced antitumor activity in both NSCLC and breast xenograft models, resulting in tumor regression and a complete inhibition of metastatic tumor spread in host animals, which may prove to be of substantial benefit to patients who currently respond suboptimally to trastuzumab therapy (page 9334, right column, first paragraph of Discussion; pages 9335-9336, Conclusion section; Figures 1 and 2).
Regarding instant claims 5 and 6, it would have been obvious for a person having ordinary skill in the art at the time of filing to modify the human albumin nanoparticle of formula X as taught by the combined teachings of Selis, Ehrlich and Yurkovetskiy to comprise a total of two decoration chains, wherein the anti-HER2 Fabs, Fab1 and Fab2, correspond to the Fab of trastuzumab and Fab of pertuzumab as taught by Scheuer. This is obvious because, the combined teachings of Selis, Ehrlich and Yurkovetskiy teach the conjugation of HSA to a peptide analogue, wherein the peptide analogue comprises a functional group 6-maleimidohexanoic acid, a glycine spacer unit, a consensus motif TQGA conjugated to the peptide linker comprising an L-lysine, and the biological molecule trastuzumab that can be used for diagnostic and therapeutic applications as an anti-cancer molecule for cancers such as human breast cancer, and Scheuer teaches that the differing mechanisms of action of trastuzumab and pertuzumab can act in a complementary fashion to provide a more complete blockade of HER2-mediated signal transduction than either agent alone, thus strongly enhancing antitumor activity in both NSCLC and breast xenograft models, resulting in tumor regression and a complete inhibition of metastatic tumor spread in host animals. Therefore, it is obvious to a skilled artisan with reasonable expectation of success to have been motivated to form the instant method for treating breast cancer comprising administering to a patient in need thereof an effective amount of human albumin nanoparticles as shown in Formula X, wherein instant R1 and R2 are two different types of Fab, Fab1 and Fab2, wherein instant Fab1 and Fab2 is trastuzumab and pertuzumab.
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, 3-10, and 12 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-10, and 13 of copending Application No. 18/039,198 (US PGPUB No. 20230414772A1; hereinafter ‘198). Although the claims at issue are not identical, they are not patentably distinct from each other. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claim 1 of ‘198 teaches serum albumin nanoparticles (Alb-NP) decorated with at least one decoration chain comprising: a linker, bound to the nanoparticles by means of an -S- thioether bond, and at least one biological molecule wherein the at least one biological molecule is bound to the linker through an amide bond formed by means of a transamidation (or transglutamination) reaction, mediated by the enzyme transglutaminase, said nanoparticles having formula I or formula II (as shown below), which is identical to instant formulas I and II (see instant claim 1).
PNG
media_image3.png
444
762
media_image3.png
Greyscale
PNG
media_image4.png
408
819
media_image4.png
Greyscale
Claims 2 and 7-10 of ‘198 further teach the Alb-NP comprising a human albumin nanoparticle (NP-HSA), a Z group deriving from a functional group, such as 6-maleimidohexanoic acid, a glycine spacer, a L-lysine amino acid, and the consensus sequence TQGA (see instant claims 3 and 7-10). Additionally, claim 3 of ‘198 teach that the nanoparticles have an average diameter (or Z-average size) of 100-500nm (see instant claim 4), and 5 and 6 of ‘198 teach that the Alb-NP comprising R1 and R2 are different from each other and are two different types of Fab, wherein the Fab is a recombinant Fab of Trastuzumab and Pertuzumab (see instant claims 5 and 6). Furthermore, claim 13 of ‘198 also disclose Formula (X), which is identical to the instant Formula (X) recited in instant claim 12.
Regarding instant claims 1, 3-10, and 12, the instant method for treating a pathology, e.g. breast cancer, comprising administering to a patient in need thereof an effective amount of Alb-NP, e.g. instant Formula X, comprises the same Alb-NP with the same limitations as described in claims 1-3, 5-10, and 13 of ‘198. A claimed product is obvious over a claimed method comprising the same product. Therefore, although the claims at issue are not identical, the instant claims are not patentably distinct from the issue claims.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Jieun Ham whose telephone number is (571)272-7779. The examiner can normally be reached Monday - Friday 7-2.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Julie can be reached at (571)272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/J.H./Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
Prosecution Insights