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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 6/18/2026 has been entered.
Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
Response to Arguments
Applicant’s arguments filed 6/18/2026, with respect to the claim rejections under 35 U.S.C. 103 based on Kim in view of Rauch, have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
Applicant’s arguments filed 6/18/2026, with respect to the claim rejections under 35 U.S.C. 103 based on Jung in view of Unson and Riber (and further in view of Han and Kim2), have been fully considered and are persuasive. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground(s) of rejection is made in view of the amended claims.
Additionally, Applicant’s request that the double patenting rejections be held in abeyance until at least one allowable claim is identified is noted but the rejections are maintained/modified herein.
Claim Status
Claims 100, 127-137 and 139-140 are pending under examination. Claims 100, 127-131, 133, 137, and 140 are currently amended. Claims 1-99, 101-126, and 138 are cancelled.
Priority
The instant application is the 371 national stage entry of PCT/KR2019/013057, filed 10/4/2019, which claims priority to KR10-2018-0118463, filed 10/4/2018, and KR10-2018-0118462, also filed 10/4/2018. The translations of KR10-2018-0118463 and KR10-2018-0118462, filed 6/18/20206, are acknowledged. The priority date of 10/4/2018 is acknowledged.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," 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 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) 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") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) 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 of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
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.
See linker sequences “[GGGS]x” and “[GGGGS]x” in [00625].
Specification
The use of the terms CONTRAVE ([0005]), OZEMPIC and TULICITY ([0822, 0824] and Figures 7-9), which are trade names or marks used in commerce, have been noted in this application. The terms should be accompanied by the generic terminology; furthermore the terms should be capitalized wherever they appear or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
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 131, 132, and 134-136 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.
Claim 131 recites “wherein a biocompatible material is linked to the peptide or wherein the biocompatible material is selected from…” (emphasis added). The scope of this claim is indefinite because it is unclear whether “a biocompatible material” is the same biocompatible material recited in the preceding claim 130 or is a different biocompatible material in addition to the one recited in claim 130. Further, by virtue of their dependency on claim 131, claims 132 and 136 are also hereby rejected for this same reasoning. For purposes of examination, “a biocompatible material” in claim 131 is being interpreted as the same biocompatible material recited in claim 130.
The term “low-molecular weight” in claim 134 is a relative term which renders the claim indefinite. The term “low-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. Further, by virtue of its dependency on claim 134, claim 135 is also hereby rejected for this same reasoning.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 100 and 127-137 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Kim et al. (US 2018/0186853 A1, effectively filed 6/30/20215, published 7/5/2018).
Kim teaches pharmaceutical compositions and methods for treating metabolic syndrome by administering to a subject in need thereof a pharmaceutical composition containing a glucagon derivative and at least one compound or material having a therapeutic activity for metabolic syndrome (co-administration; [0015, 0021, 0023]).
Regarding claim 100, Kim teaches SEQ ID NO: 37 and SEQ ID NO: 38, which correspond and are identical to the instant SEQ ID NO: 37 and SEQ ID NO: 38, respectively (Sequence Listing; Table 1).
Kim further teaches the compound or material having a therapeutic activity for metabolic syndrome can be a dipeptidyl peptidase-IV (DPP-IV) inhibitor ([0132]).
Kim also teaches metabolic syndrome is characterized in that it is selected from the group consisting of impaired glucose tolerance, hypercholesterolemia, dyslipidemia, obesity, and diabetes among others ([0156]).
Regarding claim 127, Kim teaches that both SEQ ID NO: 37 and 38 have a ring that is formed between the 16th and 20th amino acid residues from the N-terminus of the peptide (Table 1; Sequence Listing). Table 1 further demonstrates that SEQ ID NO: 37 and 38 have pI values different from the pI value of native glucagon (SEQ ID NO: 1 in Table 1).
Regarding claim 128, SEQ ID NO: 37 and 38 do not have C-terminal amidation; however, Kim further teaches the C-termini of peptides of the invention can be amidated ([0127, 0172, 0324]). The peptides of the invention are also derivatives of native glucagon that can activate the glucagon receptor ([0197-0198, 0206, 0419]).
Regarding claim 129, as stated above, Kim teaches SEQ ID NO: 37, which anticipates the instant SEQ ID NO: 37 (Sequence Listing; Table 1).
Regarding claim 130, Kim teaches an isolated conjugate comprising a glucagon derivative and a biocompatible material, which is capable of increasing in vivo half-life, are linked ([0018, 0136-0137]).
Regarding claims 131 and 132, Kim teaches the biocompatible material is selected from polyethylene glycol, fatty acid, cholesterol, albumin and a fragment thereof, an albumin-binding material, a polymer of repeating units of a particular amino acid sequence, an antibody, an antibody fragment, an FcRn-binding material, in vivo connective tissue or a derivative thereof, a nucleotide, fibronectin, transferrin, a saccharide, and a polymer ([0137]). Moreover, the polymer is selected from polyethylene glycol, polypropylene glycol, an ethylene glycol-propylene glycol copolymer, polyoxyethylated polyol, polyvinyl alcohol, a polysaccharide, dextran, polyvinyl ethyl ether, a biodegradable polymer such as polylactic acid (PLA) and polylactic-glycolic acid (PLGA), lipid polymer, chitin, hyaluronic acid, fatty acid, a polymer, a low molecular weight compound, a nucleotide, and a combination thereof ([0138]).
Regarding claim 133, Kim teaches the glucagon derivative can be linked to a biocompatible material via a linker ([0138-139, 0179-0180]).
Regarding claims 134 and 135, Kim teaches the isolated peptide is characterized in that it is linked to a biocompatible material by a linker selected from the group consisting of polyethylene glycol, polypropylene glycol, an ethylene glycol-propylene glycol copolymer, polyoxyethylated polyol, polyvinyl alcohol, a polysaccharide, dextran, polyvinyl ethyl ether, a biodegradable polymer such as polylactic acid (PLA) and polylactic-glycolic acid (PLGA), lipid polymer, chitin, hyaluronic acid, fatty acid, a polymer, a low molecular weight compound, a nucleotide, and a combination thereof. The isolated peptide and the insulinotropic peptide are respectively linked to a biocompatible material by a peptide linker or a non-peptide linker selected from the group consisting of polyethylene glycol, polypropylene glycol, an ethylene glycol-propylene glycol copolymer, polyoxyethylated polyol, polyvinyl alcohol, a polysaccharide, polyvinyl ethyl ether, dextran, a biodegradable polymer such as polylactic acid (PLA) or polylactic-glycolic acid (PLGA), lipid polymer, chitin, hyaluronic acid, and a combination thereof ([0179-0181]).
Regarding claim 136, Kim teaches the immunoglobulin Fc region comprises one selected from the group consisting of: (a) CH1 domain, CH2 domain, CH3 domain, and CH4 domain; (b) CH1 domain and CH2 domain; (c) CH1 domain and CH3 domain; (d) CH2 domain and CH3 domain; (e) a combination of one or more domains selected from the CH1 domain, CH2 domain, CH3 domain, and CH4 domain and an immunoglobulin hinge region or a part of the hinge region; and (f) a dimer of each domain of the heavy chain constant region and the light chain constant region; wherein the polypeptides comprising the immunoglobulin Fc region are in a dimeric form; wherein the immunoglobulin Fc region is a derivative of native Fc from which a region capable of forming a disulfide bond is deleted, from which some amino acids of the N-terminus are removed, to which a methionine residue of the N-terminus is added, from which a complement-binding site is removed, or from which an antibody-dependent cell-mediated cytotoxicity (ADCC) region is removed; wherein the immunoglobulin Fc region is an Fc region derived from immunoglobulin selected from the group consisting of IgG, IgA, IgD, IgE, and IgM; wherein the immunoglobulin Fc region is an IgG4 Fc region; or wherein the immunoglobulin Fc region is an aglycosylated Fc region derived from human IgG4 ([0142-0153]).
Regarding claim 137, Kim teaches the non-peptide linker is characterized in that it is linked to the cysteine residue of a peptide ([0155]). Kim also teaches the non-peptide linker is characterized in that both ends of the non-peptide linker are respectively linked to an amine group or a thiol group of a peptide and a biocompatible material ([0156]).
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.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
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.
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.
First rejection – Kim in view of Bolkent
Claim(s) 100, 127-137, and 139-140 are rejected under 35 U.S.C. 103 as being unpatentable over Kim et al. (US 2018/0186853 A1, effectively filed 6/30/20215, published 7/5/2018) in view of Bolkent et al. (EP 3 351 262 A1, published 7/25/2018).
The teachings of Kim have been set forth above. Kim does not teach the above method wherein the second compound administered is a SGLT2 inhibitor selected from the list recited in claim 139.
Bolkent teaches curaglutide, which is a proteolysis resistant GLP-1 analogue, for use in prophylaxis and/or treatment of pre-diabetes, diabetes, obesity and metabolic diseases associated thereto (Abstract; [0016, 0040]).
Bolkent further teaches curaglutide can be administered with at least one additional agent. The antidiabetic agents that can be included in the composition include empagliflozin, dapagliflozin, canagliflozin, remogliflozin, sergliflozin, tofogliflozin, and sitagliptin among others ([0018-0019]).
Based on these teachings, regarding claim 139, it would be prima facie obvious to co-administer SEQ ID NO: 37 and a SLGT2 inhibitor such as one of those taught by Bolkent, effectively substituting one therapeutic for another. Kim established that one could co-administer SEQ ID NO: 37 with additional compounds to treat metabolic syndrome. Similarly, Bolkent established treatment of metabolic syndrome and its associated symptoms with a GLP-1 and antidiabetic compound combination. Therefore, the substitution of one therapeutic for another, both of which are known to treat metabolic disorder, is obvious. See MPEP 2143(I)(B).
Regarding claim 140, as stated above, Bolkent teaches co-administration of curaglutide with empagliflozin or sitagliptin among others ([0018-0019]).
Second rejection – DiMarchi
Claim(s) 100, 127-137, and 140 are rejected under 35 U.S.C. 103 as being unpatentable over DiMarchi (US20120288511A1, published 11/15/2012).
DiMarchi teaches glucagon analogs comprising a modified amino acid sequence of native human glucagon (SEQ ID NO: 2) that exhibit activity at the glucagon receptor, activity at the GLP-1 receptor, or activity at each of the glucagon receptor and the GLP-1 receptor. Related conjugates, dimers and multimers, and pharmaceutical compositions, and uses thereof, are further provided (Abstract).
The disease or medical condition treated may be metabolic syndrome, which is characterized by a cluster of at least three or more of the following risk factors: (1) abdominal obesity (excessive fat tissue in and around the abdomen), (2) atherogenic dyslipidemia (blood fat disorders including high triglycerides, low HDL cholesterol and high LDL cholesterol that enhance the accumulation of plaque in the artery walls), (3) elevated blood pressure, (4) insulin resistance or glucose intolerance, (5) prothrombotic state (e.g., high fibrinogen or plasminogen activator inhibitor-1 in blood), and (6) pro-inflammatory state (e.g., elevated C-reactive protein in blood). Other risk factors may include aging, hormonal imbalance and genetic predisposition. The invention provides a method of preventing or treating metabolic syndrome, reducing one, two, three or more risk factors thereof, in a subject, comprising providing to the subject an analog described herein in an amount effective to prevent or treat metabolic syndrome or a risk factor thereof ([0292, 0296]).
DiMarchi teaches that the glucagon analogs described may be administered alone or in combination with other therapeutic agents which aim to treat or prevent any of the disease or medical conditions described herein. For example, the glucagon analogs may be co-administered with (simultaneously or sequentially) an anti-diabetic or anti-obesity agent, such as Dipeptidyl peptidase-4 (DPP-4) inhibitors like vildagliptin or sitagliptin ([0286]).
One glucagon analog taught by DiMarchi is SEQ ID NO: 83. The differences between the instant SEQ ID NO: 37 and SEQ ID NO: 83 of DiMarchi are 1) the amino acid at position 1 is not Tyr, 2) the amino acid at position 2 is not Ser, 3) there is no ring formed between the amino acids at positions 16 and 20, and 4) there is no Cys residue at position 30, all shown below:
PNG
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200
642
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Greyscale
However, DiMarchi further teaches substituting Ser at position 2 for AiB as well as forming an intramolecular lactam ring between lysine and glutamate residues at positions 16 and 20 to further increase the glucagon analog’s resistance to DPP-IV protease ([0161]). DiMarchi also teaches substitution of His at position 1 to Tyr in conjunction with an intramolecular bridge, such as the one described above ([0163]).
DiMarchi teaches that the glucagon analogs have an alpha helical structure, which can be stabilized by alpha helix promoting amino acids and intramolecular bonds ([0137, 0143, 0146]).
Finally, DiMarchi teaches C-terminal extensions of the glucagon analog, including adding a Cys residue to the C-terminus, wherein the Cys is optionally conjugated to a heterologous moiety ([0199-0200]).
Based on these teachings, regarding claims 100 and 129, it would be prima facie obvious to introduce the above modifications 1-4 into SEQ ID NO: 83 of DiMarchi, thereby arriving at the instant SEQ ID NO: 37. One skilled in the art would be motivated to do so and have a reasonable expectation of success because DiMarchi taught that the above described modifications increase the glucagon analog’s resistance to DPP-IV protease activity, further stabilize its structure, and provide a C-terminal extension that could easily be conjugated to additional heterologous moieties. For each and all of these reasons, it would be obvious to make the above substitutions and modifications.
Regarding claim 127, as stated above, DiMarchi teaches the formation of a ring between the 16th and 20th amino acid residues from the N-terminus of the peptide ([0146, 0161]).
Regarding claim 128, DiMarchi teaches that the glucagon analogs described are derived from native human glucagon (Abstract). DiMarchi further teaches the glucagon analog can be an amidated peptide, such that the C-terminal residue comprises an amide in place of the alpha carboxylate of an amino acid ([0179, 0213]).
Regarding claims 130-132, DiMarchi teaches conjugates of the glucagon analogs ([0071]). The glucagon analog can be conjugated to a heterologous moiety such as Fc fusions, hydrophilic moieties, rPEG, and multimers (biocompatible material; [0211]).
Regarding claim 133, DiMarchi teaches the heterologous moiety may be attached via a linker ([0234]).
Regarding claim 134-135, DiMarchi teaches the linker can be a peptide linker ([0245]). Dimarchi further teaches the linker can be PEG ([0257]).
Regarding claim 136, DiMarchi teaches Fc region may comprise one or more native or modified constant regions from an immunoglobulin heavy chain, other than CH1 for example, the CH2 and CH3 regions of IgG and IgA, or the CH3 and CH4 regions of IgE ([0246-0249]).
Regarding claim 137, as described above, DiMarchi teaches the addition of a C-terminal Cys residues to the glucagon analog, wherein the Cys is optionally conjugated to a heterologous moiety ([0199-0200]).
Regarding claim 140, DiMarchi teaches the glucagon analog can be administered in combination with a DPP-IV inhibitor such as sitagliptin ([0286]).
Claim(s) 100, 127-137, and 139-140 are rejected under 35 U.S.C. 103 as being unpatentable over DiMarchi (US20120288511A1, published 11/15/2012) in view of Bolkent et al. (EP 3 351 262 A1, published 7/25/2018).
The teachings of DiMarchi have been set forth above. DiMarchi does not teach the above method wherein the second compound administered is a SGLT2 inhibitor selected from the list recited in claims 139.
Bolkent teaches curaglutide, which is a proteolysis resistant GLP-1 analogue, for use in prophylaxis and/or treatment of pre-diabetes, diabetes, obesity and metabolic diseases associated thereto (Abstract; [0016, 0040]).
Bolkent further teaches curaglutide can be administered with at least one additional agent. The antidiabetic agents that can be included in the composition include empagliflozin, dapagliflozin, canagliflozin, remogliflozin, sergliflozin, tofogliflozin, and sitagliptin among others ([0018-0019]).
Based on these teachings, regarding claim 139, it would be prima facie obvious to co-administer SEQ ID NO: 37 and a SLGT2 inhibitor such as one of those taught by Bolkent, effectively substituting one therapeutic for another. Kim established that one could co-administer SEQ ID NO: 37 with additional compounds to treat metabolic syndrome. Similarly, Bolkent established treatment of metabolic syndrome and its associated symptoms with a GLP-1 and antidiabetic compound combination. Therefore, the substitution of one therapeutic for another, both of which are known to treat metabolic disorder, is obvious. See MPEP 2143(I)(B).
Regarding claim 140, as stated above, Bolkent teaches co-administration of curaglutide with empagliflozin or sitagliptin among others ([0018-0019]).
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 100 and 127-137 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9 and 13-18 of U.S. Patent No. 11,667,688 (US ‘688). Although the claims at issue are not identical, they are not patentably distinct from each other because practicing the instant method claims anticipates the claims of US ‘688 because SEQ ID NO: 20, 22, and 37 of US ‘688 are identical to the instant SEQ ID NO: 20, 22, and 37.
Claims 100 and 127-137 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 and 21-27 of U.S. Patent No. 10,696,725 (US ‘725). Although the claims at issue are not identical, they are not patentably distinct from each other because practicing the instant method claims anticipates the peptide, compositions, and method claims of US ‘725; the instant SEQ ID NO: 37 meets the limitations of General Formula 2 as recited in claim 1 of US ‘725.
Claims 100, 127-137, and 139-140 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-22 of U.S. Patent No. 11,142,559 (US ‘559) in view of Bolkent et al. (EP 3 351 262 A1, published 7/25/2018).
Instant SEQ ID NO: 37 meets the limitations of General Formula 2 and is identical to SEQ ID NO: 37 of US ‘559. The specification of US ‘559 indicates that the compositions containing glucagon derivatives or conjugates used for preventing or treating congenital hyperinsulinism can also be used to prevent or treat metabolic syndrome (Col. 3, lines 49-54). Therefore, the only difference between the instant claims and those of US ‘559 is the addition of an SGLT2 or DPP-IV inhibitor.
As described above, Bolkent teaches administration of GLP-1 analogues in combination with antidiabetic agents such SLGT2 or DPP-IV inhibitors. Thus, in light of the teachings of Bolkent, it would be obvious to co-administer the instant SEQ ID NO: 37 in combination with an SGLT2 or DPP-IV inhibitor. One would be motivated to do so and have a reasonable expectation of success given that Bolkent taught such methods could be used to treat diabetes, obesity, and other associated metabolic disorders. Thus, the claims of US ‘559 are obvious in view of these teachings.
Claims 100 and 127-128, 130-131, and 133-137 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No. 11,261,227 (US ‘227). Although the claims at issue are not identical, they are not patentably distinct from each other because the practicing the instant method claims anticipates the claims of US ‘227 because SEQ ID NO: 20 and 22 of US ‘227 are identical to the instant SEQ ID NO: 20 and 22.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sara E Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST.
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, Melissa L Fisher can be reached at 571-270-7430. 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.
/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
