DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 2/2/26 has been entered.
Election/Restrictions and Claim Status
Applicants’ amendments and arguments filed 2/2/26 are acknowledged.
Previously, the compound 2 as shown in Table 1 of the specification was elected.
Claims to the elected species are rejected as set forth below. Any relevant art uncovered during the search for the elected species is cited herein in order to advance prosecution.
Claims 2-9, 11 and 13 have been canceled.
Claims 1, 10, 12 and 14-18 are being examined.
Priority
This section is updated due to the addition of claims 15-18.
The priority information is found in the filing receipt dated 9/20/24.
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(a) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date under 35 U.S.C. 119(a) as follows:
The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of 35 U.S.C. 112(a) or the first paragraph of pre-AIA 35 U.S.C. 112, except for the best mode requirement. See Transco Products, Inc. v. Performance Contracting, Inc., 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994).
The disclosure of the prior-filed application, Application No. INDIA 202021026360, fails to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, first paragraph for one or more claims of this application.
Claims 15 and 16 recite dyslipidemia in the context of an effective amount. INDIA 202021026360 makes no mention of dyslipidemia.
Claims 17-18 recite a polypeptide or pharmaceutically acceptable salt thereof with certain properties. Instantly elected compound 2 is described in provisional application INDIA 202021026360 as having a half-maximal effective concentration of 40.8 nM on GLP-1R-expressing cells in a cellular cAMP assay and a half-maximal effective concentration of 23.45 nM on GIPR-expressing cells in a cellular cAMP assay (page 25) which is not consistent with what is recited in claims 17-18
As such, there is no reasonable basis to conclude that claims 15-18 are supported by INDIA 202021026360. As such, claims 15-18 have a priority date of at best 1/20/21.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 2/2/26 and 12/19/25 have been considered by the examiner.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 10, 12 and 14-18 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 1 recites moiety B and shows a structure. The structural features required by the structure are unclear. At numerous locations in the structure -NH- appears. Such depiction appears to suggest that the hydrogen is bonded to the nitrogen and something else. In contrast, US 11,866,477 (previously cited) clearly shows that the hydrogen is only bonded to the nitrogen (claim 4). Stated another way, it is unclear if
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(see claim 4 of US 11,866,477) is the same as
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(instant claims 1 and 12). None of the dependent claims clarify the claim scope.
Instant claims 17-18 recite a polypeptide or pharmaceutically acceptable salt thereof with certain properties. Instantly elected compound 2 is described in provisional application INDIA 202021026360 as having a half-maximal effective concentration of 40.8 nM on GLP-1R-expressing cells in a cellular cAMP assay and a half-maximal effective concentration of 23.45 nM on GIPR-expressing cells in a cellular cAMP assay (page 25) which is not consistent with what is reported on page 42 of the 47 page instant specification. A compound and its properties are inseparable. It is unclear how the same compound appears to have different properties and it is unclear if the elected compound reads on claims 17-18.
Although unclear, the claims have been given the broadest reasonable interpretation consistent with the specification.
Claim Rejections - 35 USC § 103
The priority of claims 15-18 is discussed above. Although Thennati et al. (US 2019/0309040; ‘Thennati’) was disqualified as prior art for certain claims, instant claims 15-18 have a different priority date.
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 15-18 is/are rejected under 35 U.S.C. 103 as being unpatentable over Bokvist et al. (US 2016/0199438 as cited with IDS 8/22/24; ‘Bokvist’) in view of Thennati et al. (US 2019/0309040; ‘Thennati’; first cited 1/16/25).
Bokvist teach peptides that agonize receptors for glucagon-like peptide-1 (GLP-1) for treating type 2 diabetes (abstract). Bokvist teach the use of fatty acids to improve pharmacokinetics by extending the half-life (section 0009). Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046). Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. In claim 15, Bokvist shows the structure of a specific peptide. Bokvist teach the compounds as part of a pharmaceutical composition (section 0047) and specifically recites the inclusion of a carrier (section 0036 and claim 12). Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1). Bokvist provides data to show the utility of the peptides (section 0112-0130). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
The compound of Bokvist does not contain the same modified lysine residue as required by claims 15-18.
Thennati teach GLP-1 analogs that have an improved duration of action where the analogs are used for treating diabetes (abstract) and specifically teach GLP-1 agonists for treating type 2 diabetes (section 0003). Thennati teach analogs that are acylated with protracting moieties which increase the duration of action (section 0002). Thennati teach improved potency of the analogs and protracting moieties with stable bonds which are less susceptible to cleavage (section 0038). Thennati specifically teach the use of a lipid modified lysine wherein the side chain (epsilon amino) group of lysine is acylated (section 0079) and teach specific moieties including moiety D (Table 1 page 7). Thennati recognizes that the length of the alkyl chain can be from 14-20 (section 0023). Thennati teach methods of preparing compounds (sections 0087-0115 and example 1).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Bokvist based on the teachings and suggestions of Bokvist. Since Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2 one would have been motivated to make compounds of such formula. Since Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046) one would have been motivated to use the known fatty acid and linkers as taught by Thennati (compare moiety D of Table 1 page 7). One would have been motivated to use the teachings of Thennati because Thennati teach the same use (treating type 2 diabetes) and teach advantages including analogs that are acylated with protracting moieties which increase the duration of action (section 0002), improve potency and have stable bonds which are less susceptible to cleavage (section 0038). Since Thennati recognizes that the length of the alkyl chain can be from 14-20 (section 0023) one would have been motivated to vary the length and include the length taught by Bokvist (claim 15). Since Bokvist teach the compounds as part of a pharmaceutical composition (section 0047) and specifically recites the inclusion of a carrier (section 0036 and claim 12) one would have been motivated to include a carrier. Since Bokvist teach effective amounts to treat dyslipidemia (section 0039) one would have been motivated to make compositions with such amounts. One would have had a reasonable expectation of success since Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1) and provides data to show the utility of the peptides (section 0112-0130). Thennati also teach methods of preparing compounds (sections 0087-0115 and example 1).
In relation to the polypeptide of claims 15-18, Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. Thennati specifically teach the use of a lipid modified lysine wherein the side chain (epsilon amino) group of lysine is acylated (section 0079) and teach specific moieties including moiety D (Table 1 page 7). When using the D moiety of Thennati as the modifying moiety in the above peptide of Bokvist the resulting peptide is the elected species which is interpreted as reading on claims 17-18.
In relation to the composition of claims 15-18, Bokvist teach the compounds as part of a pharmaceutical composition (section 0047) and specifically recites the inclusion of a carrier (section 0036 and claim 12). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 10, 12 and 14-18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 11,866,477 (477; first cited 1/16/25) in view of Bokvist et al. (US 2016/0199438 as cited with IDS 8/22/24).
477 recites a GLP-1 agonist with a specific modification (claim 1-6). 477 recites a composition with an excipient (claim 7).
477 does not recite a specific polypeptide as claimed.
Bokvist teach peptides that agonize receptors for glucagon-like peptide-1 (GLP-1) for treating type 2 diabetes (abstract). Bokvist teach the use of fatty acids to improve pharmacokinetics by extending the half-life (section 0009). Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046). Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. In claim 15, Bokvist shows the structure of a specific peptide. Bokvist teach the compounds as part of a pharmaceutical composition (section 0047) and specifically recites the inclusion of a carrier (section 0036 and claim 12). Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1). Bokvist provides data to show the utility of the peptides (section 0112-0130). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 477 because 477 expressly teach modification of a GLP-1 agonist peptide so one would have been motivated to use the known peptide sequences taught by Bokvist. Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046). Thus one would have been motivated to use the specific moiety as taught by 447 (see claim 4). Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. Since Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046) one would have been motivated to use the known fatty acid and linkers as taught by 447. Since 447 recognizes that the length of the alkyl chain can be from 14-20 (claims 4-5) one would have been motivated to vary the length and include n is 18. Since 447 teach the compounds as part of a pharmaceutical composition with an excipient (claim 7) one would have been motivated to include an excipient. Since Bokvist teach effective amounts to treat dyslipidemia (section 0039) one would have been motivated to prepare such compositions. One would have had a reasonable expectation of success since Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1) and provides data to show the utility of the peptides (section 0112-0130). Further, 447 expressly suggest GLP-1 agonist peptides (claim 1).
In relation to the polypeptide of claims 1, 10 and 12, Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. 447 teach specific modifying moieties (claims 4-5). When using the moiety of 447 as the modifying moiety in the above peptide of Bokvist the resulting peptide is the elected species which has been interpreted as reading on claims 17-18.
In relation to claims 14-18, 477 recites a composition with an excipient (claim 7). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
Claims 1, 10, 12 and 14-18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of U.S. Patent No. 12,421,289 (289) in view of Bokvist et al. (US 2016/0199438 as cited with IDS 8/22/24).
289 recites a GLP-1 agonist with a specific modification (claim 1-6). 289 recites a composition with an excipient (claim 14).
289 does not recite a specific polypeptide as claimed.
Bokvist teach peptides that agonize receptors for glucagon-like peptide-1 (GLP-1) for treating type 2 diabetes (abstract). Bokvist teach the use of fatty acids to improve pharmacokinetics by extending the half-life (section 0009). Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046). Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. In claim 15, Bokvist shows the structure of a specific peptide. Bokvist teach the compounds as part of a pharmaceutical composition (section 0047) and specifically recites the inclusion of a carrier (section 0036 and claim 12). Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1). Bokvist provides data to show the utility of the peptides (section 0112-0130). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of 289 because 289 expressly teach modification of a GLP-1 agonist peptide so one would have been motivated to use the known peptide sequences taught by Bokvist. Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046). Thus one would have been motivated to use the specific moiety as taught by 289 (see claim 2). Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. Since Bokvist teach that the fatty acid is conjugated to the epsilon amino group of a lysine side chain through a linker and that the fatty acid and linker provide the potential to generate long acting compounds (section 0046) one would have been motivated to use the known fatty acid and linkers as taught by 289. Since 289 recognizes that the length of the alkyl chain can be from 14-20 (claim 1) one would have been motivated to vary the length and include n is 18. Since 289 teach the compounds as part of a pharmaceutical composition with an excipient (claim 14) one would have been motivated to include an excipient. Since Bokvist teach effective amounts to treat dyslipidemia (section 0039) one would have been motivated to prepare such compositions. One would have had a reasonable expectation of success since Bokvist teach methods of synthesis of compounds of the invention (section 0055 and example 1) and provides data to show the utility of the peptides (section 0112-0130). Further, 289 expressly suggest GLP-1 agonist peptides (claim 1).
In relation to the polypeptide of claims 1, 10 and 12, Bokvist teach peptides of formula I (sections 0012-0013) and specifically recites an embodiment where X1 and X2 are Aib, X3 is Phe and the C-terminal amino acid is amidated and the lysine at position 20 is modified through conjugation of the epsilon amino group of lysine (section 0014 and claim 2) to result in Y(Aib)EGTFTSDYSI(Aib)LDKIAQ(modified K)AFVQWLIAGGPSSGAPPPS-NH2. 289 teach specific modifying moieties (claim 1). When using the moiety of 289 as the modifying moiety in the above peptide of Bokvist the resulting peptide is the elected species which has been interpreted as reading on claims 17-18.
In relation to claims 14-18, 289 recites a composition with an excipient (claim 14). Bokvist teach effective amounts to treat dyslipidemia (section 0039).
Response to Arguments – double patenting
Applicant's arguments filed 2/2/26 have been fully considered but they are not persuasive with respect to the rejections set forth above.
Although applicants refer to a terminal disclaimer, that terminal disclaimer was acknowledged in the advisory action of 12/9/25 but it does not apply to the rejections set forth above.
Although applicants argue about 477 alone, the rejection set forth above are not based on 477 alone.
Although applicants argue about results for tirzepatide that are different, MPEP 716.02(b) states that the burden is on the applicant to establish results are unexpected and significant. Bokvist teach the use of fatty acids to improve pharmacokinetics by extending the half-life (sections 0009 and 0046). Applicants state “relative to tirzepatide, which does not include moiety B” (page 5 of 2/2/26 reply). MPEP 716.02(c) II recognizes that expected beneficial results are evidence of obviousness. It does not appear that any comparison of the structure of tirzepatide (and/or known properties) to the instantly claimed structure are presented. It has not been set forth whether or not tirzepatide is prior art or the closest prior art (see MPEP 716.02(e) comparison with the closest prior art). MPEP 716.02 recognizes that any difference between the claimed invention and the prior art may be expected to result in differences in properties. It appears that the comparisons made are based on different concentrations. MPEP 716.02(e) expressly recognizes that: "Where the comparison is not identical with the reference disclosure, deviations therefrom should be explained, In re Finley, 174 F.2d 130, 81 USPQ 383 (CCPA 1949), and if not explained should be noted and evaluated, and if significant, explanation should be required. In re Armstrong, 280 F.2d 132, 126 USPQ 281 (CCPA 1960) (deviations from example were inconsequential)". In the instant case, there does not appear to be any comparison of the same doses. There is no discussion or evidence explaining whether or not dose dependency is linear or expected to be linear. Absent such information, one cannot ascertain if any alleged differences are due to differences in the experimental procedures or if they are truly due to the agent administered. There are inadequate facts to establish unexpected results. Further, any unexpected results are to be commensurate in scope with the claimed invention. The claimed invention broadly refers to salts thereof. There does not appear to be any data related to salts.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to RONALD T NIEBAUER whose telephone number is (571)270-3059. The examiner can normally be reached M - F 6:30 - 2:30 EST.
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RONALD T. NIEBAUER
Primary Examiner
Art Unit 1658
/RONALD T NIEBAUER/Examiner, Art Unit 1658
Prosecution Insights