CTNF 17/430,664 CTNF 95281 DETAILED ACTION Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia 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 07-42-04 AIA 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03/24/2025 has been entered. Priority This application is a 371 of PCT/US2020/017997 filed 02/12/2020. PCT/US2020/017997 has PRO 62/804,357 filed 02/12/2019. Claim Status Claims 1-18, 21, 24, 27-28, and 31-34 are pending. Claims 1, 4, 9-10, 13, 18, 31-34 are amended. Claims 19-20, 22-23, 25-26, 29-30 are canceled. Claims 1-18, 21, 24, 27-28, and 31-34 are being examined on the merits in this office action. Claim Rejections - Withdrawn The rejection of claims 1-18, 21, 24, 27-28, and 31-34 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA), first paragraph, is withdrawn in view of the claim amendments. Claim Objections - New 07-29-01 AIA Claim 1, 9, 18, and 33 are objected to because of the following informalities: Claim 1 recites “amyline” of line 6. The claim should be amended to recite “amylin”. Claim 9 recites “…conjugate having a molecular weight…”. The claim should be amended to recite “…conjugate has a molecular weight…”. Claim 18 has a similar issue. Claim 21 recites “…method of treating a subject for diabetes…”. The claim should be amended to recite “…method of treating a subject with diabetes…”. Claim 27 and 33 has a similar issue Appropriate correction is required. Claim Rejections - 35 USC § 112 - New 07-30-02 AIA 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. 07-34-01 Claims 1-18, 21, 24, 27-28, and 31-34 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. 07-34-03 AIA The term “ selective molecular weight ” in claim 1 and 10 is a relative term which renders the claim indefinite. The term “ selective molecular weight ” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. Examiner further notes that it is unclear what molecular weight is required to have the similar hydrodynamic size . Further, the term “similar hydrodynamic size” is not defined in the specification. It is unclear what the term means. Examiner looked into the instant specification and paragraph [0049] discloses that pramlintide/CB[7]-PEG complex, has a Rh 1.7 nm and aspart/CB[7]-PEG complex has a Rh 2.9 nm which do not appear to be similar. Claim 5 recites “…CB[7]-PEG prevents protein precipitation…”. It is unclear which protein applicant is referring to. Claim 33 depends on a cancelled claim 19 and is therefore indefinite since the metes and bounds are unknowable. Claim 34 depends on claim 33 and is therefore rejected as well. For examination purposes, claim 33 is construed to depend on claim 10. Claims 1-4, 6-9, 11-18, 21, 24, 27-28, and 31-32 are rejected because they depend on a rejected claim 1 or 10. Claim Rejections - 35 USC § 103 - New 07-06 AIA 15-10-15 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. 07-20-aia AIA 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. 07-20-02-aia AIA 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. 07-21-aia AIA Claims 1-5, 9-14, 18, 21, 24, 27-28, and 31-34 are r ejected under 35 U.S.C. 103 as being unpatentable over S chlein et al . (US 2009/0054305 A1 - hereinafter “Schlein”*) in view of Webber et al . (WO 2017/062622 A1 - hereinafter “Webber”*) as evidenced by Pindrus et al . (Pharm Res (2017) 34:2250–2259). * Reference attached in previous office action. Schlein teaches co-formulation of insulin and amylin [0252, 0260-0262, 0266]. Teaches insulin novolog (Insulin aspart) Humalog (insulin lispro) [0043], wherein the pH of said pharmaceutical composition or a reconstituted solution of said pharmaceutical composition is from about pH 6.5 to about pH 9.0 (claim 2; [0050, 0133-0136]). Schlein teaches amylin analogues include pramlintide [0011-0019, 0045]. Schlein further teaches that the peptides especially amylin tends to fibrillate ex-vivo and become ineffective due to precipitation and that even pramlintide is difficult to keep in solution at neutral pH and it is therefore provided in an acidic solution i.e. Symlin. [0006]. Schlein teaches that the physical stability of the insulin and/or the amylin peptide(s) in a composition of the invention can be determined by a ThT fibrillation assay for the assessment of physical stability of protein formulations [0081]. Schlein teaches formulation for subcutaneous injection at physiological pH [0267]. Schlein teaches a pharmaceutical composition combining an amylin peptide, and a meal-related insulin peptide in a stable solution in order to be able to better mimic the physiological profile of the peptides in a patient in response to glucose metabolism and limit the number of daily injections [0010], and that stabilizers used in the composition include polyethylene glycol [0032, 0087, 0096]. Schlein does not teach stabilizing the composition comprising amylin and insulin using CB[7]. However, the use of CB[7] improve the stability and duration of action of the therapeutic agent is known in the art as taught by Webber et al . Webber teaches formulating insulin with CB[7] (claims 4-6, 10-12) that supramolecular PEGylation of insulin with PEG-T-CB[7] promotes dramatically increased stability under these conditions and that at the 50-day endpoint of the study, none of the PEG-T-CB[7] formulations had aggregated at pH 7.4 [0018]. Webber teaches that insulin is well known to form fibrillar aggregates in physiologic conditions, that insulin formulated with all molecular weights of PEG-T-CB[7] did not aggregate in 100 hours of kinetic study [00236]. Webber teaches that after the initial 100 h study, data were collected once daily to determine the duration of stability for each PEG-T- CB[7]/insulin formulation (Figure 3B) and that at the 50-day endpoint of these studies, formulation of insulin with PEG 5k -T-CB[7], PEG 10k -T-CB[7], and PEG 30k -T-CB[7] remained stable and were not aggregated [00236]. Webber teaches a host such as cucurbit[7]uril (CB[7]) conjugated to a tag such PEG (claims 10-17), and that the tag improves the pharmacological properties of the agent [00153]. Webber teaches that the insulin administered with PEG-T-CB[7] inhibited aggregation of insulin [00237] and that the animals remained normoglycemic for approximately 3 hours and 5 hours following administration [00238]. Examiner notes that this teaching further reads on altering the pharmacokinetics. Examiner further notes that since Webber teaches that PEG-T-CB[7] altered the pharmacological properties of the agent (such as insulin), there is an expectation that it would similarly alter the properties of other agents such as amylin. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the pharmaceutical composition of Schlein and use CB[7] in the composition so as to stabilize and improve the pharmacokinetics of the proteins as well as so as to inhibit the formation of amyloid fibrils thus affecting the size as taught by Webber because Webber teaches that formulating insulin with CB[7] promotes dramatically increased stability under these conditions and that at the 50-day endpoint of the study, none of the PEG-T-CB[7] formulations had aggregated ([0018]; claims 4—6, 10-12). One of ordinary skill in the art would be motivated and would have had a reasonable expectation of success in adding CB[7] in the composition of Schlein because Webber teaches that supramolecular conjugates of therapeutic agents can help achieve improved stability and duration of action of the therapeutic agent [0005]. Examiner notes that regarding the limitation “having selective molecular weight” and “have similar hydrodynamic sizes”, it is known in the art that amylin and insulin have a specific molecular weight and since the molecular weight is similar, it is expected that they would have the same hydrodynamic sizes. Additionally, Examiner notes that Webber teaches that the addition of PEG-T-CB[7] inhibited aggregation of insulin [00237]. As evidenced by Pindrus, aggregation has an effect on the hydrodynamic size of a protein (Title). Specifically, Pindrus teaches that the aggregation increases the hydrodynamic size of a protein (Page 2251, left col., 1 st paragraph). Examiner notes that the addition of CB-7 would thus affect the hydrodynamic size of the protein it conjugated to thus decreasing the size to match the size the other protein in a formulation with. Further, Examiner notes that the instant claims require a composition with amylin, insulin and CB[7]. The limitation of the hydrodynamic size would naturally occur since it is an effect of the components of the claimed composition. MPEP 2111.04 states: claim scope is not limited by claim language that suggests or makes optional but does not require steps to be performed, or by claim language that does not limit a claim to a particular structure. In the instant case, the limitation expresses the intended result of the composition of claim 1 and 10 and is given little patentable weight. The disclosures render obvious claims 1, and 10. Regarding claims 2, and 11, Schlein teaches that the amylin analogue is pramlintide [0011-0019, 0045]. Regarding claims 3, and 12, Schlein teaches the insulin novolog (Insulin aspart) Humalog (insulin lispro) [0043]. Regarding claims 4 and 13, Webber teaches insulin in the concentration of 1 mg/ml with 1 equivalent of unmodified CB[7] or PEG-T-CB[7] conjugates [00245]. Examiner notes that this is a ratio of 1:1 which falls within the recited ratios. Regarding claims 5 and 14, Webber teaches that insulin is well known to form fibrillar aggregates in physiologic conditions, that insulin formulated with all molecular weights of PEG-T-CB[7] did not aggregate in 100 hours of kinetic study [00236]. Regarding claims 9 and 18, Webber teaches that the PEG in the CB7-PEG conjugate has the molecular weight of 5 kDa, 10 kDa, or 30 kDa [0016, 0023, 00137, 00161]. It would have been obvious to modify the insulin with a PEG having the MW as taught by Weber. Regarding claims 21, 27 and 33, the teaching of Schlein and Webber render obvious the instant composition. Further, Schlein teaches that the composition comprising insulin and amylin for use to treat diabetes [0123-0124]. Regarding claims 24, 28, and 34, Webber teaches treating diabetes and the composition administered to humans [00110-00111, 0065]. Regarding claims 31-32, Schlein teaches an amylin and insulin composition wherein the concentration of insulin is 0.6mM and that of amylin is 0.05 (See Fig. 3 and Example 3). Examiner notes that this a ration of 1:12 which falls within the recited ratios . 07-21-aia AIA Claims 1- 18, 21, 24, 27-28, and 31-34 are re jected under 35 U.S.C. 103 as being unpatentable over Pr estrelski et al . (US 2014/0349926 A1 - hereinafter “Prestrelski”*) in view of Webber et al . (WO 2017/062622 A1 - hereinafter “Webber”*) as evidenced by Pindrus et al . (Pharm Res (2017) 34:2250–2259). *R eference attached in previous office action. Prestrelski teaches a formulation for parenteral administration comprising insulin that comprises a pH memory between 1 to 4 or between 6 to 8 (Abstract; claim 1) and further comprising amylin (claims 21-22; [0011]). Prestrelski teaches that the formulation does not include zinc or wherein zinc present in the formulation is bound to a chelating agent (claim 14; [0011]) and that it helps in reducing the likelihood of hexamer formation [0011, 0048]. Prestrelski teaches that the formulation comprises chelating agents such as EDTA (claims 17; [0011, 0014, 0068, 0081]). Prestrelski teaches that insulin in aqueous solution is unstable, forming amyloid fibrils and degrading through water-mediated pathways and that while the hexamer structure promotes stability in solution (pH 5-8), it also hinders diffusion and subsequent absorption [0008]. Prestrelski teaches that prevent fibrillation and degradation of insulin in aqueous solution while also promoting subcutaneous absorption, insulin analogs have been developed where the amino acid sequence has been changed to reduce the propensity for self-association while preserving receptor-binding affinity [0009]. These classes of insulin are often referred to as “monomeric” insulin, but they actually exist as weakly associated hexamers [0009]. Absorption of such preparations will still be delayed because it is dependent on the diffusion and subsequent reduction in subcutaneous concentration required for the hexamer to dissociate to the dimer/monomer [0009]. Examiner notes that from the teachings of Prestrelski, the issue of amyloid fibrillation still persist. Prestrelski does not teach the use of CB[7]-PEG. Webber teaches formulating insulin with CB[7] (claims 4—6, 10-12) that supramolecular PEGylation of insulin with PEG-T-CB[7] promotes dramatically increased stability under these conditions and that at the 50-day endpoint of the study, none of the PEG-T-CB[7] formulations had aggregated at pH 7.4 [0018]. Webber teaches that insulin is well known to form fibrillar aggregates in physiologic conditions, that insulin formulated with all molecular weights of PEG-T-CB[7] did not aggregate in 100 hours of kinetic study [00236]. Webber teaches that after the initial 100 h study, data were collected once daily to determine the duration of stability for each PEG-T- CB[7]/insulin formulation (Figure 3B) and that at the 50-day endpoint of these studies, formulation of insulin with PEG 5k -T-CB[7], PEG 10k -T-CB[7], and PEG 30k -T-CB[7] remained stable and were not aggregated [00236]. Webber teaches a host such as cucurbit[7]uril (CB[7]) conjugated to a tag such PEG (claims 10-17), and that the tag improves the pharmacological properties of the agent [00153]. Webber teaches that the insulin administered with PEG-T-CB[7] inhibited aggregation of insulin [00237] and that the animals remained normoglycemic for approximately 3 hours and 5 hours following administration [00238]. Examiner notes that this teaching further reads on altering the pharmacokinetics. Examiner further notes that since Webber teaches that PEG-T-CB[7] altered the pharmacological properties of the agent (such as insulin), there is an expectation that it would similarly alter the properties of other agents such as amylin. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the pharmaceutical composition of Prestrelski and use CB[7] in the composition so as to inhibit the formation of amyloid fibrils as taught by Webber because Webber teaches that formulating insulin with CB[7] reduced aggregation and promotes dramatically increased stability under these conditions and that at the 50-day endpoint of the study, none of the PEG-T-CB[7] formulations had aggregated ([0018]; claims 4—6, 10-12). One of ordinary skill in the art would be motivated and would have had a reasonable expectation of success in adding CB[7] in the composition of Prestrelski because Webber teaches that supramolecular conjugates of therapeutic agents can help achieve improved stability and duration of action of the therapeutic agent [0005]. Examiner notes that regarding the limitation “having selective molecular weight” and “have similar hydrodynamic sizes”, it is known in the art that amylin and insulin have a specific molecular weight and since the molecular weight is similar, it is expected that they would have the same hydrodynamic sizes. Additionally, Examiner notes that Webber teaches that the addition of PEG-T-CB[7] inhibited aggregation of insulin [00237]. As evidenced by Pindrus, aggregation has an effect on the hydrodynamic size of a protein (Title). Specifically, Pindrus teaches that the aggregation increases the hydrodynamic size of a protein (Page 2251, left col., 1 st paragraph). Examiner notes that the addition of CB-7 would thus affect the hydrodynamic size of the protein it conjugated to thus decreasing the size to match the size the other protein in a formulation with. Further, Examiner notes that the instant claims require a composition with amylin, insulin and CB[7]. The limitation of the hydrodynamic size would naturally occur since it is an effect of the components of the claimed composition. MPEP 2111.04 states: claim scope is not limited by claim language that suggests or makes optional but does not require steps to be performed, or by claim language that does not limit a claim to a particular structure. In the instant case, the limitation expresses the intended result of the composition of claim 1 and is given little patentable weight. The disclosures render obvious claims 1, and 10. Regarding claims 2, and 11, Prestrelski teaches that the amylin analog is pramlintide ([0011, 0013]; claims 22-24). Regarding claims 3, and 12, Prestrelski teaches that the insulin analog includes Lispro®, Aspart® [0017, 0049, 0113]. Regarding claims 4 and 13, Webber teaches insulin in the concentration of 1 mg/ml with 1 equivalent of unmodified CB[7] or PEG-T-CB[7] conjugates [00245]. Examiner notes that this is a ratio of 1:1 which falls within the recited ratios. Regarding claims 5 and 14, Webber teaches that insulin is well known to form fibrillar aggregates in physiologic conditions, that insulin formulated with all molecular weights of PEG-T-CB[7] did not aggregate in 100 hours of kinetic study [00236]. Regarding claims 6-8, 15-17, Prestrelski teaches that the formulation does not include zinc or wherein zinc present in the formulation is bound to a chelating agent (claim 14; [0011]) and that it helps in reducing the likelihood of hexamer formation [0011, 0048]. Prestrelski teaches that the formulation comprises chelating agents such as EDTA (claims 17; [0011, 0014, 0068, 0081]). Prestrelski teaches that zinc present in the formulation is bound to a chelating agent (claim 14; [0011]) and that the chelating agents such as EDTA is present in the amount of 1 mM [0081, 0083, 0085, 0087]. One of ordinary skill in the art would be motivated to include zinc and EDTA in the same ratio so as to avoid hexamer formation as taught by Prestrelski in [0011]. Regarding claims 9 and 18, Webber teaches that the PEG in the CB7-PEG conjugate has the molecular weight of 5 kDa, 10 kDa, or 30 kDa [0016, 0023, 00137, 00161]. It would have been obvious to modify the insulin with a PEG having the MW as taught by Weber. Regarding claim 21, 27, and 33, Prestrelski teaches a method of reducing blood glucose level comprising administering to a subject in need thereof any one of the formulations and that the subject has diabetes [0012]. Regarding claim 24, 28, and 34, Prestrelski teaches that the subject is a human [0012]. Regarding claims 31-32, Prestrelski teaches a ratio of 5:1 (w/w) insulin:pramlintide [0131] which falls within the instant ratios . Response to Arguments 07-37 AIA Applicant's arguments filed 08/01/2025 have been fully considered but they are not persuasive. Applicant’s Arguments Applicant argues that Examiner fails to present any prima facie case of obviousness and that the references do not teach all the claim limitations. Applicant argues that the claim have been amended to recite “similar hydrodynamic size of the protein…”. Applicant argues that Schlein does not teach or suggest the use of any CB[7]-PEG that could optimize the pharmacokinetics of insulin and amylin simultaneous in vivo as claimed. Applicant argues that Prestrelsky is incompatible with Webber and irrelevant and that Webber does not teach hydrodynamic size of protein and CB-7 conjugate in formulation. Applicant argues that neither reference describes a moiety provided in effective amount to alter the pharmacokinetics of the amylin element and the insulin element to more closely match each other". (Arguments Page 7-8). Examiner’s Response The arguments presented above have been fully considered but are unpersuasive. First, Examiners wishes to remind Applicant that the obviousness rejection based on the combined teachings of Schlein and Webber. In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller , 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). The test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. See In re Keller , 642 F.2d 413, 208 USPQ 871 (CCPA 1981). Secondly, a composition that comprises Amylin and Insulin is known in the art as taught by Schelin. What the Schlein reference does not teach, is the addition of CB[7]-PEG and the motivation to do so. However, the addition of CB[7]-PEG in pharmaceutical composition is known in the art as taught by Webber. In fact, the main reason for the addition of CB[7]-PEG is to prevent aggregation of the protein drug. The instant specification discloses that the large dissimilarity in pharmacokinetics arises from the distinct aggregation states of the proteins in formulation and the resulting impact on absorption behavior [0010, 0011]. The instant specification further discloses that CB[7]-PEG further stabilizes insulin thus altering the pharmacokinetics of the hormone [0044]. Examiner notes this is exactly what Webber teaches; that CB[7]-PEG stabilizes insulin and prevents aggregation, specifically Webber teaches a host such as cucurbit[7]uril (CB[7]) conjugated to a tag such PEG (claims 10-17), and that the tag improves the pharmacological properties of the agent [00153]. Webber teaches that the insulin administered with PEG-T-CB[7] inhibited aggregation of insulin [00237] and that the animals remained normoglycemic for approximately 3 hours and 5 hours following administration [00238]. It is therefore evident from the teachings of Webber that the inclusion of CB[7]-PEG indeed alters the pharmacokinetics of the hormone. Examiner further notes that the composition of the instant invention requires three components; Amylin, Insulin and CB[7]-PEG. This composition has been rendered obvious by the cited references and specifically, one of ordinary skill in the art has the motivation to add CB[7]-PEG since Webber teaches that it prevents aggregation, stabilizes the hormone and thus improves the pharmacokinetics of the hormone. Examiner further adds that the limitation “…similar hydrodynamic size…” is a result effect of the components of the claimed invention. Examiner notes that the addition of CB[7]-PEG is known to affect the hydrodynamic size of the protein since CB[7]-PEG directly prevents aggregation of the protein drug. It is known in the art that aggregation affects the hydrodynamic size of the protein as disclosed by Pindrus et al . Additionally, since this limitation is a result of the components claimed, it is worth noting that the MPEP 2111.04 states: claim scope is not limited by claim language that suggests or makes optional but does not require steps to be performed, or by claim language that does not limit a claim to a particular structure. In the instant case, the limitation expresses the intended result of the composition of claim 1 and 10 and is given little patentable weight. Thus the argument regarding the Webber reference are unpersuasive. With regards to the argument of the Schlein reference, Examiner notes that the reference is relevant to the rejection because Schlein teaches co-formulation of insulin and amylin [0252, 0260-0262, 0266]. Teaches insulin novolog (Insulin aspart) Humalog (insulin lispro) [0043], wherein the pH of said pharmaceutical composition or a reconstituted solution of said pharmaceutical composition is from about pH 6.5 to about pH 9.0 (claim 2; [0050, 0133-0136]). Schlein teaches amylin analogues include pramlintide [0011-0019, 0045]. Schlein does not teach the addition of CB7, but this limitation is satisfied by the Webber reference. The argument is unpersuasive. With regards to the argument that the Prestrelsky reference is irrelevant, Examiner disagrees. Examiner notes that Prestrelski teaches a formulation for parenteral administration comprising insulin that comprises a pH memory between 1 to 4 or between 6 to 8 (Abstract; claim 1) and further comprising amylin (claims 21-22; [0011]). Prestrelski teaches that the formulation does not include zinc or wherein zinc present in the formulation is bound to a chelating agent (claim 14; [0011]). Prestrelski does not teach the use of CB[7]-PEG, but this limitation is satisfied by the Webber reference. The argument is unpersuasive. Double Patenting 08-33 AIA 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 1-4, 6, 10-13, 15, 21, 27, 33 are still provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 41, 42, 44, 48, 51, 53, 55-56 , 58 of copending Application No. 17/784,907. Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of the copending application recite a pharmaceutical composition comprising insulin or an insulin analog; an optionally substituted cucurbit[7]uril (CB[7])-polyethylene glycol (PEG) conjugate (claim 41), the pharmaceutical composition of claim 41, further comprising at least one of: amylin or an amylin analogue, or amylin or an amylin analogue comprising pramlintide (claim 53). The claims of the instant application recite a pharmaceutical composition comprising: amylin or an amylin analogue; insulin or an insulin analogue; and a cucurbit [7] uril (CB[7])-poly(ethylene glycol) (PEG) conjugate in an effective amount sufficient to inhibit formation of amyloid fibrils (claim 1, 10). Regarding the limitation of “..having selective molecular weight” and “similar hydrodynamic size..” Examiner notes that the limitation is an intended or expected result of the claimed composition. Further, the copending application recites the molecular weight of the CB-7-PEG conjugate thus recites the molecular weight. Regarding claim 2, 11, the claims of the copending application recites amylin or an amylin analogue, or amylin or an amylin analogue comprising pramlintide (claim 53). Regarding claim 3, 12, the claims of the copending application recites an insulin analog selected from the group consisting of insulin aspart, insulin lispro (claim 42). Regarding claim 4, 13, the claims of the copending application recites wherein at least one of:the molar ratio of CB [7]-PEG to the insulin or insulin analogue is from about 1:1 to about 10, or the molar ratio of CB[7]-PEG to the insulin or insulin analogue is from about 3:1 to about 5:1 (claim 51). Regarding claim 6, 15, the claims of the copending application recites the pharmaceutical composition is substantially free of zinc (claim 48). Regarding claim 9, 18, the claims of the copending application recites wherein the PEG has a molecular weight of less than about 1 kDa, from about 1 to about 10 kDa, from about 5 to about 10 kDa, from about 10 to about 30 kDa, more than about 30 kDa, or less than about 100 kDa (claim 46). Regarding claim 21, 27, 33, the claims of the copending application recites a method of managing or reducing blood glucose level in a subject (claim 55), wherein the subject has either type 1 diabetes or type 2 diabetes (claim 56-58) This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Response to Arguments Applicant did not respond to this rejection. As a result, the rejection is maintained. Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Mercy H. Sabila whose telephone number is (571)272-2562. The examiner can normally be reached Monday - Friday 5:00 am - 3:00 pm. 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, Lianko G. Garyu can be reached at (571)270-7367. 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. /MERCY H SABILA/Examiner, Art Unit 1654 /LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654 Application/Control Number: 17/430,664 Page 2 Art Unit: 1654 Application/Control Number: 17/430,664 Page 3 Art Unit: 1654 Application/Control Number: 17/430,664 Page 4 Art Unit: 1654 Application/Control Number: 17/430,664 Page 5 Art Unit: 1654 Application/Control Number: 17/430,664 Page 6 Art Unit: 1654 Application/Control Number: 17/430,664 Page 7 Art Unit: 1654 Application/Control Number: 17/430,664 Page 8 Art Unit: 1654 Application/Control Number: 17/430,664 Page 9 Art Unit: 1654 Application/Control Number: 17/430,664 Page 10 Art Unit: 1654 Application/Control Number: 17/430,664 Page 11 Art Unit: 1654 Application/Control Number: 17/430,664 Page 12 Art Unit: 1654 Application/Control Number: 17/430,664 Page 13 Art Unit: 1654 Application/Control Number: 17/430,664 Page 14 Art Unit: 1654 Application/Control Number: 17/430,664 Page 15 Art Unit: 1654 Application/Control Number: 17/430,664 Page 16 Art Unit: 1654 Application/Control Number: 17/430,664 Page 17 Art Unit: 1654 Application/Control Number: 17/430,664 Page 18 Art Unit: 1654 Application/Control Number: 17/430,664 Page 19 Art Unit: 1654 Application/Control Number: 17/430,664 Page 20 Art Unit: 1654 Application/Control Number: 17/430,664 Page 21 Art Unit: 1654 Application/Control Number: 17/430,664 Page 22 Art Unit: 1654
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