DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. 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 for the cited rejections 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.
3. Response to Election/Restriction filed on 4/27/2026 is acknowledged.
4. Claim filed on 4/27/2026 is acknowledged.
5. Claims 2, 14 and 15 have been cancelled.
6. Claims 1, 3-13 and 16-24 are pending in this application.
7. Claims 3, 7-9, 11 and 17 are withdrawn from consideration as being drawn to non-elected species.
8. Claims 1, 4-6, 10, 12, 13, 16 and 18-24 are under examination.
Priority
9. The application is a 371 of PCT/IB2021/000044 filed on 1/29/2021, which claims priority to US provisional application No. 62/968594 filed on 1/31/2020. US provisional application No. 62/968594 fails to provide support to instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 for at least the following reason: It does not disclose the dosage of “from 0.08 mg/kg to 1 mg/kg” recited in instant claim 1. Therefore, the effective filing date of instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 is 1/29/2021.
Election/Restrictions
10. Applicant’s election without traverse of a pharmaceutical composition that comprises a mutant FGF-21 peptide conjugate having the structure:
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, wherein n is an integer selected from 450 to 460; wherein the mutant FGF-21 peptide (FGF-21 in the structure above) consists of the amino acid sequence set forth in SEQ ID NO: 2; wherein the mutant FGF-21 peptide is attached by a covalent bond at a threonine at amino acid position 173 of SEQ ID NO: 2; wherein the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG; and wherein the pharmaceutical composition does not comprise a weight loss therapeutic agent as species of pharmaceutical composition; a subject, wherein the subject is not afflicted with diabetes, NASH, and/or metabolic syndrome and wherein the subject has a BMI ranging from 25 to less than 30 as species of subject; and reduction of total body weight as species of effect of treatment in the reply filed on 4/27/2026 is acknowledged. The requirement is made FINAL in this office action.
The instant claims 1, 3-13 and 16-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof. A search was conducted on the elected species; and prior art was found. Claims 3, 7-9, 11 and 17 are withdrawn from consideration as being drawn to non-elected species. Claims 1, 4-6, 10, 12, 13, 16 and 18-24 are examined on the merits in this office action.
Objections
11. The specification is objected to for the following minor informality: The specification discloses various chemical structures/formulas on pages 32-43 of instant specification. However, the quality of these chemical structures/formulas is extremely poor. Applicant is required to provide clear image for these chemical structures/formulas.
Please note: The specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification (see MPEP § 608.01).
12. The drawings are objected to for the following minor informality:
Figures 1-28 are described with respect to color. Reference to specific colors in the description of the drawings should be removed.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
13. Claim 1 is objected to for the following minor informality: Applicant is suggested to amend claim 1 as “A method for reduction of total body weight, body fat content, body mass index (BMI), or combinations thereof in a subject in need thereof, wherein the method comprises administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, and wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between threonine at position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety, and the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG”.
14. Claim 5 is objected to for the following minor informality: Claim 5 contains the acronym “NASH”. An acronym in the first instance of claims should be expanded upon/spelled out with the acronym indicated in parentheses, for example, non-alcoholic steatohepatitis (NASH). The abbreviation can be used thereafter.
15. Claim 19 is objected to for the following minor informality: Applicant is suggested to amend claim 19 as “…wherein the 20 kDa PEG moiety is attached to the glycosyl moiety via a linker, and wherein the linker…”.
16. Claim 21 is objected to for the following minor informality: Applicant is suggested to amend claim 21 as “…wherein the mutant FGF-21 peptide conjugate comprises the structure -GalNAc-Sia-Gly-PEG of 20 kDa”.
17. Claim 22 is objected to for the following minor informality: Applicant is suggested to amend claim 22 as “…wherein the mutant FGF-21 peptide conjugate comprises the structure:
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, and wherein n is…”.
Furthermore, Applicant is required to provide a better and clear image of the recited structure.
Rejections
Claim Rejections - 35 U.S.C. § 112 paragraph (b)
18. 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.
19. Claim 12 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
20. Claim 12 recites “The method of claim 1, wherein the pharmaceutical composition is administered sub-subcutaneously”. With regards to the term “sub-subcutaneously”, the instant specification fails to define it. And such term is not known and/or commonly used in the medical art. Therefore, it is unclear what is encompassed within the recited “sub-subcutaneously”. Thus, the metes and bounds of instant claim 12 is vague and indefinite.
Furthermore, for the purpose of this examination, the Examiner is interpretating the recited “sub-subcutaneously” as “subcutaneously”. Such interpretation applies to all the rejections set forth below.
Claim Rejections - 35 U.S.C. § 112 paragraph (d)
21. The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), fourth paragraph:
Subject to the [fifth paragraph of 35 U.S.C. 112 (pre-AIA )], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
22. Claim 23 is rejected under 35 U.S.C. 112(d) or 35 U.S.C. 112 (pre-AIA ), 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
23. Claim 23 depends on claim 1; and claim 23 recites “The method of claim 1, wherein the 20 kDa PEG is a linear or branched PEG”. However, the 20 kDa PEG recited in instant claim 1 can only be either a linear PEG or a branched PEG. Therefore, the scope of the 20 kDa PEG recited in instant claim 23 is identical to the scope of the 20 kDa PEG recited in claim 1. Claim 23 does not further limit the structure of the 20 kDa PEG in claim 1; therefore, claim 23 is improper dependent forms for failing to further limit the subject matter of claim 1.
Claim Rejections - 35 U.S.C. § 103
24. 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 of this title, 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.
25. The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 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.
26. Claims 1, 4-6, 10, 12, 13, 16 and 18-24 are rejected under 35 U.S.C. 103 as being unpatentable over Kopec et al (US 2019/0185533 A1, filed with IDS) in view of Sanada et al (Intern Med, 2012, 51, pages 1821-1826).
The instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof.
Kopec et al, throughout the patent, teach a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate comprising: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2 (identical to the mutant FGF-21 peptide of instant SEQ ID NO: 2), ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between threonine at position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety, and the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein the mutant FGF-21 peptide conjugate has an improved half-life of about 80 hours in humans, and wherein the mutant FGF-21 peptide conjugate comprises the structure
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with n being an integer selected from 450 to 460; and a method for treating diabetes or a diabetes related disease, in particular diabetes type 2, non-alcoholic steatohepatitis (NASH) or metabolic syndrome, wherein the method comprise administering to a subject in need thereof an amount of a pharmaceutical composition comprising such mutant FGF-21 peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is human, wherein the mutant FGF-21 peptide conjugate is administered once a week or once every two weeks, and wherein the administration results in reduction of total weight, for example, Abstract; page 1, paragraph [0004] to page 2, paragraph [0015]; page 3, paragraphs [0024] and [0025]; page 4, paragraph [0026]; page 18, paragraph [0198]; page 21, paragraphs [0242] and [0245]; and claims 1-19. It reads on a pharmaceutical composition that comprises a mutant FGF-21 peptide conjugate having the structure:
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, wherein n is an integer selected from 450 to 460; wherein the mutant FGF-21 peptide (FGF-21 in the structure above) consists of the amino acid sequence set forth in SEQ ID NO: 2; wherein the mutant FGF-21 peptide is attached by a covalent bond at a threonine at amino acid position 173 of SEQ ID NO: 2; wherein the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG; and wherein the pharmaceutical composition does not comprise a weight loss therapeutic agent as the elected species of pharmaceutical composition; and reduction of total body weight as the elected species of effect of treatment. It meets the limitations of the subject, the effect of treatment, the pharmaceutical composition and the administration scheme recited in instant claims 1, 4, 10, 13, 16 and 18-24. Kopec et al further teach such method can be for prophylactic treatment, for example, page 17, paragraph [0196]. Therefore, one of ordinary skilled in the art would understand and immediately envision that the subject in the method for prophylactic treatment in Kopec et al is one not afflicted with diabetes, NASH and/or metabolic syndrome. It meets the limitations of instant claim 5. Kopec et al also teach the pharmaceutical composition is administered subcutaneously, for example, page 7, paragraph [0081]; and page 17, paragraph [0196]. It meets the limitations of instant claim 12. Furthermore, Kopec et al teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight; and efficacious doses range from 0.1 mg/kg to 6 mg/kg when tested in various animal models of NASH and type 2 diabetes, for example, pages 17-18, paragraph [0197].
The difference between the reference and instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 is that the reference does not explicitly teach a subject, wherein the subject is not afflicted with diabetes, NASH, and/or metabolic syndrome and wherein the subject has a BMI ranging from 25 to less than 30 as the elected species of subject; the dosage recited in instant claim 1; and the limitations of instant claim 6.
However, Sanada et al, throughout the literature, teach overweight/obesity (high BMI) is an independent and dose-dependent risk factor for type 2 diabetes; and the Hazard ratios for diabetes mellitus is 3.12 for those with a BMI of 25-27.4 and it is increased to 3.80 for participants with a BMI of 27.5 or higher, for example, Abstract; page 1823, Table 2; and page 1824, Figure 1 and Table 3.
Furthermore, one of ordinary skilled in the art would have been motivated to optimize the dosage of the mutant FGF-21 peptide conjugate for better efficacy, including a dosage of from 0.08 mg/kg to 1 mg/kg, because Kopec et al teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight. And the MPEP states the following: 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) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc. v. Biocraft Laboratories Inc., 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert. denied, 493 U.S. 975 (1989); In re Kulling, 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler, 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997) (see MPEP § 2144.05 II A).
Therefore, it would have been obvious to one of ordinary skilled in the art to combine the teachings of Kopec et al and Sanada et al with routine optimization to develop a method for reduction of total body weight in a human subject having type 2 diabetes or a human subject having a BMI of 25-27.4 (at high risk for having type 2 diabetes), wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG. It reads on a subject, wherein the subject is not afflicted with diabetes, NASH, and/or metabolic syndrome and wherein the subject has a BMI ranging from 25 to less than 30 as the elected species of subject.
One of ordinary skilled in the art would have been motivated to combine the teachings of Kopec et al and Sanada et al with routine optimization to develop a method for reduction of total body weight in a human subject having type 2 diabetes or a human subject having a BMI of 25-27.4 (at high risk for having type 2 diabetes), wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG, because Sanada et al, throughout the literature, teach overweight/obesity (high BMI) is an independent and dose-dependent risk factor for type 2 diabetes; and the Hazard ratios for diabetes mellitus is 3.12 for those with a BMI of 25-27.4 and it is increased to 3.80 for participants with a BMI of 27.5 or higher. Furthermore, one of ordinary skilled in the art would have been motivated to optimize the dosage of the mutant FGF-21 peptide conjugate for better efficacy, including a dosage of from 0.08 mg/kg to 1 mg/kg, because Kopec et al teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight. And the MPEP states the following: “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” (see MPEP § 2144.05 II A).
A person of ordinary skilled in the art would have reasonable expectation of success in combining the teachings of Kopec et al and Sanada et al with routine optimization to develop a method for reduction of total body weight in a human subject having type 2 diabetes or a human subject having a BMI of 25-27.4 (at high risk for having type 2 diabetes), wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG.
27. Please note: During the search for the elected species, prior art was found for the non-elected species of subject.
Claims 1, 4, 5, 10, 12, 13, 16 and 18-24 are rejected under 35 U.S.C. 103 as being unpatentable over Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) in view of Kopec et al (US 2019/0185533 A1, filed with IDS).
The instant claims 1, 4, 5, 10, 12, 13, 16 and 18-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof.
Coskun et al, throughout the literature, teach a method for reduction of total body weight in diet-induced obese (DIO) mice, wherein the method comprises subcutaneously administering to the mice a pharmaceutical composition comprising fibroblast growth factor-21 (FGF-21) peptide and a pharmaceutically acceptable carrier, wherein the FGF-21 is administered at a dose of 0.1, 0.3, or 1mg/kg, for example, Abstract; page 6018, right column, the 1st paragraph and Section “Animals”; page 6019, Section “FGF21 ameliorates obese phenotypes in DIO and ob/ob mice”; and page 6020, Figure 1A. It reads on reduction of total body weight as the elected species of effect of treatment. It meets the limitations of the subject, dosage, and the effect of treatment recited in instant claim 1; and the limitations of instant claim 12. Coskun et al further teach FGF21 half-life in mice is only about 1 h, thus, the uninterrupted activation of FGF21 signaling is required to achieve maximal weight-lowering effect, for example, page 6025, left column, the 3rd paragraph.
The difference between the reference and instant claims 1, 4, 5, 10, 12, 13, 16 and 18-24 is that the reference does not explicitly teach a pharmaceutical composition that comprises a mutant FGF-21 peptide conjugate having the structure:
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, wherein n is an integer selected from 450 to 460; wherein the mutant FGF-21 peptide (FGF-21 in the structure above) consists of the amino acid sequence set forth in SEQ ID NO: 2; wherein the mutant FGF-21 peptide is attached by a covalent bond at a threonine at amino acid position 173 of SEQ ID NO: 2; wherein the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG; and wherein the pharmaceutical composition does not comprise a weight loss therapeutic agent as the elected species of pharmaceutical composition; the limitations of the mutant FGF-21 peptide conjugate recited in instant claim 1; and the limitations of instant claims 4, 5, 10, 13, 16 and 18-24.
However, Kopec et al, throughout the patent, teach a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate comprising: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2 (identical to the mutant FGF-21 peptide of instant SEQ ID NO: 2), ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between threonine at position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety, and the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein the mutant FGF-21 peptide conjugate has an improved half-life of about 80 hours in humans, and wherein the mutant FGF-21 peptide conjugate comprises the structure
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with n being an integer selected from 450 to 460; and a method for prophylactic and/or therapeutical treatment of diabetes or a diabetes related disease, in particular diabetes type 2, non-alcoholic steatohepatitis (NASH) or metabolic syndrome, wherein the method comprise administering to a subject in need thereof an amount of a pharmaceutical composition comprising such mutant FGF-21 peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is human, wherein the mutant FGF-21 peptide conjugate is administered once a week or once every two weeks, and wherein the administration results in reduction of total weight, for example, Abstract; page 1, paragraph [0004] to page 2, paragraph [0015]; page 3, paragraphs [0024] and [0025]; page 4, paragraph [0026]; page 17, paragraph [0196]; page 18, paragraph [0198]; page 21, paragraphs [0242] and [0245]; and claims 1-19. It reads on a pharmaceutical composition that comprises a mutant FGF-21 peptide conjugate having the structure:
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, wherein n is an integer selected from 450 to 460; wherein the mutant FGF-21 peptide (FGF-21 in the structure above) consists of the amino acid sequence set forth in SEQ ID NO: 2; wherein the mutant FGF-21 peptide is attached by a covalent bond at a threonine at amino acid position 173 of SEQ ID NO: 2; wherein the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG; and wherein the pharmaceutical composition does not comprise a weight loss therapeutic agent as the elected species of pharmaceutical composition. Kopec et al further teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight, for example, pages 17-18, paragraph [0197].
Furthermore, one of ordinary skilled in the art would have been motivated to optimize the dosage of the mutant FGF-21 peptide conjugate for better efficacy, including a dosage of from 0.08 mg/kg to 1 mg/kg, because Kopec et al teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight. And the MPEP states the following: 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) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc. v. Biocraft Laboratories Inc., 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert. denied, 493 U.S. 975 (1989); In re Kulling, 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler, 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997) (see MPEP § 2144.05 II A).
Therefore, it would have been obvious to one of ordinary skilled in the art to combine the teachings of Coskun et al and Kopec et al with routine optimization to develop a method for reduction of total body weight in an obese mice or human subject, wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG.
One of ordinary skilled in the art would have been motivated to combine the teachings of Coskun et al and Kopec et al with routine optimization to develop a method for reduction of total body weight in an obese mice or human subject, wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG, because Kopec et al, throughout the patent, teach a mutant FGF-21 peptide conjugate comprising: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2 (identical to the mutant FGF-21 peptide of instant SEQ ID NO: 2), ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between threonine at position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety, and the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein the mutant FGF-21 peptide conjugate has an improved half-life of about 80 hours in humans, and wherein the mutant FGF-21 peptide conjugate comprises the structure
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with n being an integer selected from 450 to 460; and a method for prophylactic and/or therapeutical treatment of diabetes or a diabetes related disease, in particular diabetes type 2, non-alcoholic steatohepatitis (NASH) or metabolic syndrome, wherein the method comprise administering to a subject in need thereof an amount of a pharmaceutical composition comprising such mutant FGF-21 peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is human, wherein the mutant FGF-21 peptide conjugate is administered once a week or once every two weeks, and wherein the administration results in reduction of total weight. Furthermore, one of ordinary skilled in the art would have been motivated to optimize the dosage of the mutant FGF-21 peptide conjugate for better efficacy, including a dosage of from 0.08 mg/kg to 1 mg/kg, because Kopec et al teach the dosage of the therapeutically effective amount of the mutant FGF-21 peptide conjugate depends the patient's state of health and weight. And the MPEP states the following: “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” (see MPEP § 2144.05 II A).
A person of ordinary skilled in the art would have reasonable expectation of success in combining the teachings of Coskun et al and Kopec et al with routine optimization to develop a method for reduction of total body weight in an obese mice or human subject, wherein the method comprises subcutaneously administering to the subject once a week or once every two weeks a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant fibroblast growth factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier; and wherein the mutant FGF-21 peptide conjugate has the structure:
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with n being an integer selected from 450 to 460, the mutant FGF-21 peptide consists of the amino acid sequence of SEQ ID NO: 2, the -GalNAc-Sia-Gly-PEG moiety is attached to position 173 of SEQ ID NO: 2 via a Gly linker, and the PEG moiety (CH3(OCH2CH2)n-) is a linear 20 kDa methoxy-PEG.
Obviousness Double Patenting
28. 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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form 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 http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
29. Claims 1, 4-6, 10, 12, 13, 16 and 18-24 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-13 of US patent 11596669 B2 and in view of Kopec et al (US 2019/0185533 A1, filed with IDS) and Sanada et al (Intern Med, 2012, 51, pages 1821-1826).
30. Instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof.
31. Claims 1-13 of US patent 11596669 B2 are drawn to:
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.
32. The difference between instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 and claims 1-13 of US patent 11596669 B2 is that claims 1-13 of US patent 11596669 B2 do not teach apply the composition recited in claims 1-13 of US patent 11596669 B2 in the method recited in instant claims.
However, in view of the combined teachings of Kopec et al and Sanada et al with routine optimization as set forth in Section 26 above, it would have been obvious to one of ordinary skilled in the art to apply the composition recited in claims 1-13 of US patent 11596669 B2 and develop the method recited in instant claims 1, 4-6, 10, 12, 13, 16 and 18-24.
Please note: US patent 11596669 B2 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
33. For the same and/or similar reasoning/rational as the rejection set forth in Sections 29-32 above, instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-20 of US patent 11850275 B2, and claims 1-9 of US patent 12350314 B2; and in view of the combined teachings of Kopec et al (US 2019/0185533 A1, filed with IDS) and Sanada et al (Intern Med, 2012, 51, pages 1821-1826) with routine optimization as set forth in Section 26 above.
Please note: US patent 11850275 B2, US patent 12350314 B2 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
34. For the same and/or similar reasoning/rational as the rejection set forth in Sections 29-32 above, instant claims 1, 4, 5, 10, 12, 13, 16 and 18-24 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-13 of US patent 11596669 B2, claims 1-20 of US patent 11850275, and claims 1-9 of US patent 12350314 B2; and in view of the combined teachings of Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS) with routine optimization as set forth in Section 27 above.
35. For the same and/or similar reasoning/rational as the rejection set forth in Sections 29-32 above, instant claims 1, 4-6, 10, 12, 13, 16 and 18-24 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-16 of co-pending Application No. 19/226706; and in view of the combined teachings of Kopec et al (US 2019/0185533 A1, filed with IDS) and Sanada et al (Intern Med, 2012, 51, pages 1821-1826) with routine optimization as set forth in Section 26 above.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Please note: co-pending Application No. 19/226706 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
36. For the same and/or similar reasoning/rational as the rejection set forth in Sections 29-32 above, instant claims 1, 4, 5, 10, 12, 13, 16 and 18-24 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-16 of co-pending Application No. 19/226706; and in view of the combined teachings of Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS) with routine optimization as set forth in Section 27 above.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
37. Claims 1, 4, 10, 12, 13, 16 and 18-24 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-27 of US 12036284 B2 and in view of Christian et al (Am J Cardiol, 2011, 107, pages 891-897), Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS).
38. Instant claims 1, 4, 10, 12, 13, 16 and 18-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof.
39. Claims 1-27 of US 12036284 B2 are drawn to various methods of treating severe hypertriglyceridemia (SHTG) in a subject in need thereof, comprising: administering once a week or once every two weeks to the subject in need thereof a pharmaceutical composition comprising a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, and wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl 20 moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG.
40. The difference between instant claims 1, 4, 10, 12, 13, 16 and 18-24 and claims 1-27 of US 12036284 B2 is that claims 1-27 of US 12036284 B2 do not explicitly teach the method recited in instant claims 1, 4, 10, 12, 13, 16 and 18-24.
However, Christian et al teach subject having SHTG is one in need of reduction of total body weight, for example, page 893, Table 2; and page 896, Table 3.
Therefore, in view of the teachings of Christian et al and the combined teachings of Coskun et al and Kopec et al with routine optimization as set forth in Section 27 above, it would have been obvious to one of ordinary skilled in the art to modify the methods recited in claims 1-27 of US 12036284 B2 and develop the method recited in instant claims 1, 4, 10, 12, 13, 16 and 18-24.
Please note: US 12036284 B2 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
41. For the same and/or similar reasoning/rational as the rejection set forth in Sections 37-40 above, instant claims 1, 4, 10, 12, 13, 16 and 18-24 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-16 of co-pending Application No. 18/733382; and in view of the teachings of Christian et al (Am J Cardiol, 2011, 107, pages 891-897) as set forth in Section 40 above and the combined teachings of Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS) with routine optimization as set forth in Section 27 above.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Please note: co-pending Application No. 18/733382 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
42. Claims 1, 4, 10, 12, 13, 16 and 18-24 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 3-15, 17-19 and 21-35 of co-pending Application No. 19/102634 and in view of Kim et al (Clinical Gastroenterology and Hepatology, 2019, 17, pages 543-550), Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS).
43. Instant claims 1, 4, 10, 12, 13, 16 and 18-24 are drawn to a method, comprising: administering once a week or once every two weeks to a subject in need thereof a pharmaceutical composition comprising from 0.08 mg/kg to 1 mg/kg of a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, wherein the subject is in need of reduction of total body weight, reduction of body fat content, reduction of body mass index (BMI), or combinations thereof, wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising an amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG, wherein administration of the pharmaceutical composition results in at least one of: reduction of total body weight, reduction of body fat content, reduction of BMI of the subject or combination thereof.
44. Claims 1, 3-15, 17-19 and 21-35 of co-pending Application No. 19/102634 are drawn to various methods of treating nonalcoholic steatohepatitis (NASH) in a subject in need thereof, comprising: administering once a week or once every two weeks to the subject in need thereof a pharmaceutical composition comprising a mutant Fibroblast Growth Factor-21 (FGF-21) peptide conjugate and a pharmaceutically acceptable carrier, and wherein the mutant FGF-21 peptide conjugate comprises: i) a mutant FGF-21 peptide comprising the amino acid sequence of SEQ ID NO: 2, ii) a glycosyl moiety, and iii) a 20 kDa polyethylene glycol (PEG), wherein the mutant FGF-21 peptide is attached to the glycosyl moiety by a covalent bond between a threonine at amino acid position 173 of SEQ ID NO: 2 and a first site of the glycosyl moiety and wherein the glycosyl 20 moiety is attached to the 20 kDa PEG by a covalent bond between a second site of the glycosyl moiety and the 20 kDa PEG.
45. The difference between instant claims 1, 4, 10, 12, 13, 16 and 18-24 and claims 1, 3-15, 17-19 and 21-35 of co-pending Application No. 19/102634 is that claims 1, 3-15, 17-19 and 21-35 of co-pending Application No. 19/102634 do not explicitly teach the method recited in instant claims 1, 4, 10, 12, 13, 16 and 18-24.
However, Kim et al teach subject having NASH is one in need of reduction of total body weight, for example, page 548, the 3rd paragraph in Section “Discussion”.
Therefore, in view of the teachings of Kim et al and the combined teachings of Coskun et al and Kopec et al with routine optimization as set forth in Section 27 above, it would have been obvious to one of ordinary skilled in the art to modify the methods recited in claims 1, 3-15, 17-19 and 21-35 of co-pending Application No. 19/102634 and develop the method recited in instant claims 1, 4, 10, 12, 13, 16 and 18-24.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Please note: co-pending Application No. 19/102634 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
46. For the same and/or similar reasoning/rational as the rejection set forth in Sections 42-45 above, instant claims 1, 4, 10, 12, 13, 16 and 18-24 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-14 of co-pending Application No. 19/512478; and in view of the teachings of Kim et al (Clinical Gastroenterology and Hepatology, 2019, 17, pages 543-550) as set forth in Section 45 above and the combined teachings of Coskun et al (Endocrinology, 2008, 149, pages 6018-6027) and Kopec et al (US 2019/0185533 A1, filed with IDS) with routine optimization as set forth in Section 27 above.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Please note: co-pending Application No. 19/512478 and instant application share the same Applicant (89BIO, INC., San Francisco, CA (US)).
Examiner’s Notes
47. The Examiner would like to bring Applicant’s attention to the following patents and US Application, which have 89Bio Ltd., Herzliya (IL) as Applicant: US patents 10407479 B2, 11427623 B1 and 12037376 B2; and US application Nos: 19/018376 and 19/086868. In the event that Applicant has provided evidence that 89Bio Ltd., Herzliya (IL) is the same as 89BIO, INC., San Francisco, CA (US) (the instant Applicant), the instant claims would be rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims of these US patents and US applications in the same and/or similar manner as the rejections set forth in Sections 29-46 above.
Conclusion
No claim is allowed.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658
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