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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 2/25/2026 has been entered.
Claim Status
Claims 1, 17, 27, and 33-35 are pending.
Claims 2-16 and 28-32 are cancelled.
Claim 17 remains withdrawn as being directed to a non-elected species. The species election of CPBM as Fc-III was made of record dated 7/31/2023 without traverse. The elected species is rejected under the modified 35 U.S.C. 103 in this office action.
Claims 1, 27, and 33-35 have been examined.
Priority
This application is a CON of 17/695,645 filed on 03/15/2022
17/695,645 is a CIP of 17/046,221 filed on 10/08/2020
17/046,221 is a 371 of PCT/US2019/026260 filed on 04/08/2019
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 2/25/2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Maintained Rejection
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.
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, 27, and 35 are rejected under 35 U.S.C. 103 as being unpatentable over (i) Khorev et al. (Bioorganic & Medicinal Chemistry 16 (2008) 5216–5231, previously cited 9/11/2023) in view of (ii) Sesarman et al. (Cell. Mol. Life Sci. (2010) 67:2533–2550, previously cited 10/20/2025), (iii) Sockolosky et al. (PLoS ONE. 2014; 9(7): e102566, previously cited 10/20/2025) evidenced by Choe et al. (Materials. 2016, 9(12), 994, previously cited 9/11/2023), and (iv) Sampler et al. (J Polym Sci A Polym Chem. 2016 Sep 15;54(18):2888-2895, previously cited 9/11/2023) in view of Kolb et al. (Drug Discov Today Actions. 2003 Dec 15;8(24):1128-37, previously cited 10/20/2025).
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Claim 1 is drawn to a compound structure as follows.
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Khorev et al. teach Trivalent, Gal/GalNAc-containing ligands designed for the asialoglycoprotein receptor as a carrier for site-specific delivery to the liver (Title and Abstract). Khorev et al. teach asialoglycoprotein receptor is to maintain serum glycoprotein homeostasis for degradation of internalized proteins (p5216, col 1, Introduction para 1). Khorev et al. further teach only the terminal residues are necessary for specific recognition, and that the binding process proceeds through a simultaneous interaction of 2–3 sugar residues with 2–3 binding sites of the heterooligomeric receptor of asialoglycoprotein receptor/ASGP-R (p5216, col 2, last para bridging to p5217, col 1, para 1) shown in figure 1 above. Khorev et al. show a liver-specific Trivalent targeting moiety
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compound 4 comprising a functionalized PEG linker for conjugation as follows (p5218, Fig 2, compound 4), reading on the claimed CRBM moiety and R2 = AcNH = (CH3CO)-NH as follows.
Khorev et al. do not teach the CRBM further conjugated to an IgG binding moiety to internalize IgG into liver cells for degradation.
Sesarman et al. teach IgG-mediated autoimmune diseases and high-affinity IgG autoantibodies are likely to be the inducers of tissue damage in several of these diseases (Table 1). Sesarman et al. further show various IgG-mediated autoimmune diseases known in the art (p2536, Table 2). Thus, one of ordinary skill in the art would have found it obvious to conjugate an IgG binding moiety to Khorev’s Trivalent Gal/GalNAc-containing ligands targeted to asialoglycoprotein receptor to internalize disease-related IgG into liver cells for degradation.
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Khorev et al. in view of Sesarman et al. do not specify an IgG binding moiety as Fc-III.
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Sockolosky et al. teach fusion of a short peptide of Fc-III that binds immunoglobulin G. Sockolosky et al. show the IgG binding peptide sequence consisting of DCAWHLGELVWCT (p2, Fig 1a-1b shown as follows) reading on the elected species CPBM of Fc-III as evidenced by the cyclic peptide structure taught by Choe et al. shown as follows (p5, Fig 2). Because Sockolosky et al. in view of Choe et al. teach beneficial fusion of the peptide of Fc-III at the D residue via a linker to a compound for non-covalent binding to IgG in vivo (p2, Fig 1a and 1b), one of ordinary skill in the art would have found it obvious to conjugate Sockolosky’s and Choe’s Fc-III (CPBM) to Khorev’s trivalent compound ligand (CRBM) at the D residue of Fc-III via a linker for degradation of internalized autoimmune disease-related IgG in liver cells to treat autoimmune diseases.
Khorev et al. in view of Sesarman et al., Sockolosky et al. and evidenced by Choe et al. do not specify how to functionalize Sockolosky’s peptide of Fc-III for click chemistry conjugation to Khorev’s trivalent compound.
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Semple et al. teach poly(ethylene glycol) (PEG) derivatives have been applied in bioconjugation chemistry through the modification of peptides and proteins; and have found broad use in immunology, virology, and drug delivery systems. The beneficial incorporation of PEG-containing moieties (PEGylation) into such systems generally improves pharmacological properties including increased water solubility, enhanced resistance to protein hydrolysis/ degradation, improved bioavailability (circulation half-life), and reduced antigenicity. Semple et al. suggest the use of click chemistry of cycloaddition between an azide and an alkyne to form a 1,2,3-triazole linkage (p2888, col 1) shown in scheme 1 (p2889) as follows. Semple et al. further teach functionalization of PEG with a click chemistry reactive group for site-specific conjugation to a compound as common knowledge known in the field of bioconjugation (p2892, Scheme 2). Knob et al. is further cited to demonstrate click chemistry between azide and alkyne for bioconjugation is well known to one of ordinary skill in the art shown as follows (p1135, Fig 4a).
Sockolosky et al. and Choe et al. teach beneficial fusion of the cyclic peptide of Fc-III at the D residue via a linker to a compound for non-covalently binding to IgG in vivo (p2, Fig 1a and 1b).
Sesarman et al. further show various IgG-mediated autoimmune diseases known in the art (p2536, Table 1-2).
Khorev et al. show triantennary ligands targeted to ASGP-R below (p5218, Fig 2), suggesting that the linking spacer comprising an alkyl chain substituted with oxygen (e.g., PEG)
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and/or amide bond do not significantly affect the terminal galactose and N-acetylgalactosamine binding to Asialoglycoprotein receptors of hepatocytes.
Semple et al. teach poly(ethylene glycol) (PEG) derivatives have been applied in bioconjugation chemistry through the modification of peptides and proteins. Semple et al. teach the beneficial incorporation of PEG-containing moieties (PEGylation) into such systems generally improves pharmacological properties including increased water solubility, enhanced resistance to protein hydrolysis/degradation, improved bioavailability (circulation half-life), and reduced antigenicity. Semple et al. suggest the use of click chemistry of cycloaddition between an azide and an alkyne to form a 1,2,3-triazole linkage (p2888, col 1) to form a conjugate shown in scheme 1 (p2889). Knob et al. is further cited to demonstrate click chemistry between azide and alkyne for bioconjugation is well known to one of ordinary skill in the art (p1135, Fig 4a).
According to the combination of (a), (b), (c), and (d), one of ordinary skill in the art would have found it obvious to fuse the cyclic IgG binding peptide of Sockolosky’s and Choe’s Fc-III (CPBM) to Khorev’s trivalent compound ligand (CRBM) targeted to liver cells via click chemistry reaction taught by Semple et al. in view of Knob et al. to generate a conjugate shown as follows, reading on the
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claimed linker X2 = -CH2-, X1=O, n= 2, m = 1, and j ≥ 1 (see Semple’s compound 1e shown
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above compared to the claimed linker below).
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Khorev’s trivalent compound ligand (CRBM) targeted to the asialoglycoprotein receptor for protein degradation with (ii) Sesarman’s teaching of IgG-mediated autoimmune diseases, and (iii) Sockolosky’s and Choe’s cyclic IgG binding peptide of Fc-III (CPBM) because (a) Khorev et al. teach asialoglycoprotein receptor is to maintain serum glycoprotein homeostasis for degradation of internalized proteins (p5216, col 1, Introduction para 1) and further show a recombinant Trivalent Gal/GalNAc-containing ligand functionalized with a PEG linker designed as a carrier for site-specific delivery to the liver (p5218, Fig 4), (b) Sesarman et al. teach IgG-mediated autoimmune diseases (p2536, Table 2), and (c) Sockolosky et al. and Choe et al. teach fusion of a short peptide of Fc-III consisting of the peptide sequence DCAWHLGELVWCT (p2, Fig 1a-1b) that specifically binds to immunoglobulin G in vivo. Choe et al. is cited as evidence to show the cyclic peptide structure of Sockolosky’s and Choe’s Fc-III (p5, Fig 2). The combination would have reasonable expectation of success because Khorev’s Trivalent Gal/GalNAc-containing ligand fusion with Sockolosk’s and Choe’s IgG binding peptide of Fc-III via a linker is capable of binding to autoimmune disease related IgG for degradation of the bound and internalized IgG in liver cells.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Khorev et al. in view of Sesarman et al., Sockolosky et al. and evidenced by Choe et al. with (ii) Sampler’s PEG linker functionalized by a click chemistry reactive group because (a) Khorev et al. in view of Sesarman et al., Sockolosky et al. and evidenced by Choe et al. teach a PEG functionalized trivalent compound (CRBM) linked to an IgG binding peptide via a linker and (b) Semple et al. teach beneficial use of a click chemistry reactive group functionalized PEG linker for site-specific conjugation to improve bioavailability (circulation half-life) and reduced antigenicity (p2888, col 1). The combination would have reasonable expectation of success because (a) functionalization of compounds and PEG linkers with azide and alkyne for click chemistry is well known in the art (e.g., Semple et al. p2889, scheme 1), (b) beneficial incorporation of PEG-containing moieties (PEGylation) generally improves pharmacological properties including increased water solubility, enhanced resistance to protein hydrolysis/ degradation, improved bioavailability (circulation half-life), and reduced antigenicity also well known in the art (p2888, col 1, p2888, col 1), and (c) fusion of Sockolosky’s IgG binding peptide of Fc-III to Khorev’s liver-targeted trivalent compound ligand (CRBM) via a click chemistry reactive group functionalized linker is expected to internalize bound IgG for degradation in liver cells to treat IgG mediated autoimmune diseases. Knob et al. is further cited to demonstrate click chemistry between azide and alkyne for bioconjugation is well known to one of ordinary skill in the art (p1135, Fig 4a). See the rejection above in details.
With respect to claim 27, Khorev et al. in view of Sockolosky et al. and evidenced by Choe et al. teach a compound of claim 1. Khorev et al. teach the use of a buffering agent of Hepes as an excipient with a compound containing Khorev’s trivalent compound/CRBM (p5229, col 1, Sec 5.21.1).
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable and can be determined by routine experimentation. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A). Indeed, the specification defines the term "effective" is used herein, unless otherwise indicated, to describe an amount of a compound or composition which, in context, is used to produce or effect an intended result, whether that result relates to the inhibition of the effects of a disease state on a subject or the treatment or prophylaxis of a subject for secondary conditions (p31, line 8-16).
Applicant’s Arguments
Khorev shows compounds 1-4 and compounds 5a/5b; thus, the examiner cited compound 4 for the rejection is impermissible by pick and choose to combine other references (Remarks, p8, last 3 para) because Khorev’s teachings are limited to ASGP-R specific uptake of fluorescently labeled compounds into hepatic cells, including into HepG2 cells and into SK-Hepl cells. However, the claimed compounds and the cited art are directed to wholly different problems (Remarks, p8 to p10, para 1).
IgG has been identified as being involved in autoimmune disease, but there is no teaching in the prior art on how to address this issue therapeutically. Sesarman notes that there is "no approach specifically targeting FcRn that is currently approved for the treatment of IgG mediated autoimmune diseases" and none of Sesarman approaches relates to degradation of IgG and hence removal of IgG from circulation (Remarks, p10, para 3).
Sockolosky et al. do not show Fc-III structure. Sockalosky describes only Fc-III connected to another protein (mKate) through a peptide linker made by recombinant DNA technology, there is absolutely no disclosure in Sockalosky, Sesarman, and Khorev of the claimed linker between Fc-III and CRBM (Remarks, p10, last 2 para to p12, para 1-2).
Sockalosky as a whole is directed to the concept that "genetic modification of recombinant proteins with short peptides that bind abundant serum proteins, such as albumin or IgG, is a general strategy to improve protein pharmacokinetics." Sockalosky (together with Sesarman and Khorev) is considered as a whole for what it fairly discloses, it is evident that its central unambiguous purpose is to increase the serum half-life of a therapeutic agent. This aim is the opposite of the therapeutic mode of action of the claimed compounds, which seek to remove a targeted IgG autoantibody from circulation and to degrade it in the liver (Remarks, p12, last para to p13, para 1).
There is no meaningful way to combine the teaching of Choe with Khorev, Sesarman, and Sockalosky to render the pending claims prima facie obvious for at least the following reasons (a) Choe states that other researchers reported "a substantial increase of the half-life of recombinant proteins that are fused to the Fc-binding protein Fc-III.", (b) Even if the Z33 peptide in Choe's hybrid molecule 10 were substituted with Fc-III, Choe' s "Triazole linker" is completely different from the claimed linker, (c) Choe's hybrid molecule 10 binds to Herceptin (the antibody), and the antibody-drug conjugate binds to the antibody's target on the cell, thereby delivering the cytotoxic agent to the cancer. This protocol cannot work if the "bioactive agent" is the recited CRBM (p13, p13, para 2-5 to p15, para 1-2).
Semple is cited for describing bioconjugation with PEG derivatives and for describing click-chemistry. Kolb is cited for describing click-chemistry between an azide and an alkyne. Chang is cited for describing certain lengths of PEG linkers and for click-chemistry. Semple, Kolb, and Chang do not cure the defects in Khorev, Sesarman, and Sockalosky noted above (Remarks, p15, para 3).
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive for the reasons as follows.
Applicant’s argument (i) is not persuasive because (A) Khorev et al. explicitly show compound 4 of Fig 2 as a Trivalent Gal/GalNAc-containing ligands targeted to the asialoglycoprotein receptor in a limited choice of homologous compounds; thus, there is no picking and choosing of the compound 4 to combine other relevant references as argued by applicant and (B) applicant improperly limit Khorev’s teaching to examples (e.g., Fig 4). Khorev’s example of ASGP-R specific uptake of fluorescently labeled compounds into hepatic cells demonstrates a Trivalent Gal/GalNAc-containing ligand (e.g., compound 4) can be used as a carrier for site-specific targeting to asialoglycoprotein receptor expressed by liver cells and internalization of the conjugated moiety into liver cells (Abstract). Thus, one of ordinary skill in the art would conjugate an IgG binding peptide of Fc-III to a Trivalent Gal/GalNAc-containing ligand (e.g., compound 4) for internalization of diseases associated IgG into liver cells for degradation as taught by the combined references described above not repeated here. A reference may be relied upon for all that it would have reasonably suggested to one having ordinary skill in the art, including nonpreferred embodiments. Merck & Co. v. Biocraft Labs., Inc. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir. 1989), cert. denied, 493 U.S. 975 (1989). See MPEP 2123. Furthermore, MPEP 2144(IV) states “Rationale different from applicant’s is permissible”; namely, the reason to combine or modify a reference does not have to be the same as applicant’s reasons of invention.
Applicant’s argument (ii) is not persuasive because (A) Khorev et al. teach the use of Trivalent Gal/GalNAc-containing ligands targeted to the asialoglycoprotein receptor expressed by liver cells to internalize a bound serum protein for degradation (Title and p5216, col 1, para 1). Thus, one of ordinary skill in the art would have found it obvious to combine the cited references described above not repeated here. (B) Combination of prior art references do not need to be approved treatment as argued by applicant. The rationale to modify or combine the prior art does not have to be expressly stated in the prior art; the rationale may be expressly or impliedly contained in the prior art or it may be reasoned from knowledge generally available to one of ordinary skill in the art, established scientific principles, or legal precedent established by prior case law. In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988); In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992). See MPEP 2144.
Applicant’s argument (iii) is not persuasive because Sockolosky et al. show the IgG binding peptide primary sequence consisting of DCAWHLGELVWCT (p2, Fig 1a-1b shown as follows) reading on the elected species CPBM of Fc-III which is the cyclic peptide structure as taught by Choe et al. (p5, Fig 2). Furthermore, Khorev et al. teach a non-peptide linker can be made by chemical synthesis for conjugation (p5219, scheme 1) when recombinant DNA technology is not suitable for use. A person of ordinary skill in the art is well defined as a person of ordinary creativity able to fit the teachings of multiple patents together like pieces of a puzzle.” Id. Office personnel may also take into account “the inferences and creative steps that a person of ordinary skill in the art would employ.” Id. at ___, 82 USPQ2d at 1396. See MPEP 2141.03 (I).
Applicant’s argument (iv) is not persuasive because one of ordinary skill in the art would have known to remove disease associated IgG from serum for degradation by conjugate Fc-III to Khorev’s Trivalent Gal/GalNAc-containing ligands targeted to the asialoglycoprotein receptor for degradation of disease associated IgG in liver cells according to the combined references. Increase of a compound’s half-life by binding to IgG via an IgG binding peptide of Fc-III as argued by applicant is another way of using the IgG binding peptide of Fc-III. One of ordinary skill in the art as defined by MPEP 2141.03 (I) would follow the teachings of cited prior art references by conjugation of Fc-III to Khorev’s Trivalent Gal/GalNAc-containing ligands (e.g., compound 4) for degradation of disease associated IgG in liver cells, not increase half-life disease associated IgG as argued by applicant.
Applicant’s argument (v) is not persuasive because (a) see response to argument (iv) above, (b) the click chemistry linker is taught by Semple et al. in view of Knob et al. (see page 6 above), not Choe' s "Triazole linker" as argued by applicant, (c) Choe’s references is cited to show the cyclic peptide structure of Fc-III as IgG binding peptide known in the art. When Choe’s IgG binding peptide of Fc-III conjugated to Khorev’s Trivalent Gal/GalNAc-containing ligands targeted to the asialoglycoprotein receptor via click chemistry linker reads on the instant compound as described above not repeated here.
Applicant’s argument (vi) is not persuasive because Semple, Kolb, and Chang are cited to show either click chemistry reaction or functionalized PEG linker for click chemistry well known to one of ordinary skill in the art. Thus, the linking moiety of CON-Linker-CON in between CPBM and CRBM is known to one of ordinary skill in the art according to Semple, Kolb, and Chang.
2. Claims 1, 27, and 33-35 are rejected under 35 U.S.C. 103 as being unpatentable over Khorev et al. in view of Sesarman et al., Sockolosky et al., Sampler et al., Kolb et al. and evidenced by Choe et al. as applied to claims 1, 27, 35 and further in view of Chang et al. (WO 2018/166529 A1, previously cited 10/20/2025).
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Claims 33-34 are drawn to 3 repeating units of PEG (j=3) in the linker shown as follows
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Khorev et al. in view of Sesarman et al., Sockolosky et al., Sampler et al., Kolb et al. and evidenced by Choe et al. teach a Fc-III conjugated to a triantennary ligand as follows, but do not specify the linker comprising 3 PEG repeating units (j = 3).
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Chang et al. teach linker units and molecular constructs (Title). Chang et al. teach the length of a PEG chain can be optimized between 2 to 20 [0126, line 25]. Chang et al. further suggest beneficial functionalization of a compound with a click chemistry reactive group using a short PEG3 linker [0138, line 15-16]; thus, one of ordinary skill in the art would have found it obvious to use PEG3 spacer for functionalization of a click chemistry reactive group reading on j =3 in claims 33-34. Therefore, the cited references teach a compound obvious to the elected compound of Fc-III-GN3 comprising PEG3 functionalized with a click chemistry reactive group for conjugation to another click chemistry reactive group functionalized IgG binding peptide of FC-III shown above.
One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Khorev et al. in view of Sesarman et al., Sockolosky et al., Sampler et al., Kolb et al. and evidenced by Choe et al. with (ii) Chang’s teaching the length of a PEG chain because (a) Khorev et al. in view of Sesarman et al., Sockolosky et al., Sampler et al., Kolb et al. teach a conjugate comprising a PEG linker functionalized with a click chemistry reactive group and (b) Chang et al. suggest beneficial functionalization of a compound with a click chemistry reactive group using a short PEG3 linker [0138, line 15-16]. The combination would have reasonable expectation of success because the references teach functionalized PEG with a click chemistry reactive group for covalent conjugation of two moieties well known in the art.
Maintained Rejection
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, 27, and 33-35 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5, and 13-14 of U.S. Patent No. 11,767,301 B2 (the ‘301 patent). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘301 patent claims the elected species of FC-III-GN3.
Claim 1 of the ‘301 patent disclosed a peptide conjugate as follows.
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Claim 1 further disclosed the IgGBM is Fc-III, FcBP-1, FcBP-2, or Fc-III-4c.
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Claim 1 further disclosed a CON comprising a triazole moiety.
Claim 5 of the ‘301 patent disclosed ASGPRAM structure as follows.
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Claim 13 of the ‘301 patent disclosed the elected compound species FC-III-GN3 as follows.
Claim 14 of the ‘301 patent disclosed a pharmaceutical composition comprising an effective amount of the conjugate in combination with a pharmaceutically acceptable carrier, additive, or excipient, satisfying the instant claim 27.
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A).
Thus, claims 1, 5, and 13-14 of the ‘301 patent is obvious to the instant claims 1, 27, and 33-35.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive because the request of this rejection held in abeyance until allowable claims are indicated does not overcome this ODP rejection of record.
Claims 1, 27, and 33-35 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 18-19 of U.S. Patent No. 12,083,181 B2 (the ‘181 patent). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘181 patent claims the elected species of FC-III-GN3.
Claim 1 of the ‘181 patent disclosed a peptide conjugate as follows.
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Claim 1 further disclosed the IgGBM is Fc-III, FcBP-1, FcBP-2, or Fc-III-4c.
Claim 18 of the ‘181 patent disclosed the elected compound species FC-III-GN3 as follows.
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Claim 19 of the ‘181 patent disclosed a pharmaceutical composition comprising an effective amount of the conjugate in combination with a pharmaceutically acceptable carrier, additive, or excipient, satisfying the instant claim 27.
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A).
Thus, claims 1 and 18-19 of the ‘181 patent is obvious to the instant claims 1, 27, and 33-35.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive because the request of this rejection held in abeyance until allowable claims are indicated does not overcome this ODP rejection of record.
Claims 1, 27, and 33-35 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 and 31-32 of copending Application No. 17/695,259 (the ‘259 application, 10/17/2025, NOA dated 3/13/2026). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘259 application is obvious to the instant application.
Claim 1 of the ‘259 application disclosed a compound comprising Fc-III conjugated to a cell-targeting moiety of ASGPRBM via a linking moiety.
Claim 2 of the ‘259 application disclosed ASGPRBM with linking moiety of claim 1.
Claims 31-32 of the ‘259 application disclosed the structure of linking moiety of the compound in claim 1.
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A).
Thus, claims 1-2 and 31-32 of the ‘259 application are obvious to the instant claims 1, 27, and 33-35.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive because the request of this rejection held in abeyance until allowable claims are indicated does not overcome this ODP rejection of record.
Claims 1, 27, and 33-35 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13 of copending Application No. 18/446,296 (the ‘296 application, 8/8/2023). Although the claims at issue are not identical, they are not patentably distinct from each other because the ‘296 application is obvious to the instant application.
Claim 1 of the ‘296 application disclosed a peptide conjugate as follows.
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Claim 1 further disclosed the CPBM is Fc-III, FcBP-1, FcBP-2, or Fc-III-4c.
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Claim 11 of the ‘296 application disclosed the elected compound species FCIII-GN3 as follows.
Claim 13 of the ‘296 application disclosed a pharmaceutical composition comprising the conjugate and at least one pharmaceutically acceptable carrier, additive, or excipient, satisfying the instant claim 27.
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A).
Thus, claims 1, 11, and 13 of the ‘296 application are obvious to the instant claims 1, 27, and 33-35.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive because the request of this rejection held in abeyance until allowable claims are indicated does not overcome this ODP rejection of record.
5. Claims 1, 27, and 33-35 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 29, 37, and 40-41 of copending Application No. 18/806,178 (the ‘178 application, 3/13/2025) in view of Sockolosky et al. (PLoS ONE. 2014; 9(7): e102566) evidenced by Choe et al. (Materials. 2016, 9(12), 994, previously cited 9/11/2023).
Claim 29 of the ‘178 application disclosed an immunoglobulin G binding compound as follows.
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Claim 29 of the ‘178 application further disclosed linker comprising a PEG spacer and a triazole click chemistry linker as follows.
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Claim 37 of the ‘178 application disclosed R2 moiety as AcNH.
Claim 40 of the ‘178 application disclosed a structure of ASGPRGM as follows.
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Claims 29, 37 and 40 of the ‘178 application did not disclose an IgG binding moiety.
Sockolosky et al. teach fusion of a short peptide of Fc-III that binds immunoglobulin G. Sockolosky et al. show the IgG binding peptide sequence consisting of DCAWHLGELVWCT (p2, Fig 1a-1b shown as follows) with 100% identity to the claimed CPBM of FcIII as evidenced by the cyclic peptide structure taught by Choe et al. (p5, Fig 2).
Because Sockolosky et al. show the IgG binding peptide sequence consisting of DCAWHLGELVWCT can be conjugate to a moiety for binding to IgG, one of ordinary skill in the art would have found it obvious to conjugate Sockolosky’s IgG binding peptide to ASGPRGM via a hybrid linker comprising PEG and triazole disclosed in claims 29, 37, and 40 of the ‘178 application described above.
Thus, claims 29, 37, and 40 of the ‘178 in view of Sockolosky et al. and Choe et al. are obvious to the instant claims 1 and 33.
Claim 41 of the ‘178 application disclosed a pharmaceutical composition comprising an effective amount of the conjugate in combination with a pharmaceutically acceptable carrier, additive, or excipient, further satisfying the instant claims 27 and 34.
With respect to claim 35, the effective dosage of a therapeutic compound is a result effective variable. Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See MPEP 2144.05 (II)(A).
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 2/25/2026 have been fully considered but they are not persuasive because the request of this rejection held in abeyance until allowable claims are indicated does not overcome this ODP rejection of record.
Conclusion
No claim is allowed.
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/J.L/Examiner, Art Unit 1658
18-April-2026
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
Prosecution Insights