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 .
Information Disclosure Statement
Filed information disclosure statements (IDS) comply with the provisions of 37 CFR 1.97, 1.98 and MPEP § 609. Accordingly, they have been placed in the application file, and the information therein has been considered as to the merits.
Status of the application
Please note that for internal reasons to USPTO, this application has been reassigned.
Receipt of applicant’s remarks and claim amendments filed on 07/02/2026 are acknowledged.
Examiner also acknowledges applicants filed sequence listing. Accordingly, previous sequence non-compliance is withdrawn.
In light of applicants arguments and claim amendments, previous 112(a), 112(b) and 102 rejections are withdrawn.
However, applicants’ arguments for the previous 103 rejections are found not persuasive. Accordingly, the previous rejections are maintained and modified to address claim amendments.
Previous nonstatutory double patenting rejections are also maintained in absence of filed terminal disclaimers, and in light of applicants request to hold the rejection in abeyance until allowable claims have been identified.
Applicants are reminded that previous restriction requirement and election of species are remain effective. Amended claims are examined in light of elected species on merits in this office action. Accordingly, newly added claims 78-79 are withdrawn, as it does not read elected SEQ ID NO:2.
Response to Arguments
(i) Applicants’ argue that the amended claims are patentable over Veiga in view of Cascales. Independent claim 1 is amended to include topically administering to a target site associated with a fungal contamination a peptide configured to self-assemble into a hydrogel in an amount effective to eliminate or reduce a target fungal organism associated with the contamination. Veiga fails to teach or suggest elimination or reduction of a fungal organism with the claimed self-assembling peptide.
Though Veiga silent on topical administration and elimination of reduction of a fungal organism, as explained in the rejection, Cascales cures these deficiencies, see With regard to claim 1 in the rejections.
(ii) Applicants argue that Cascales is cited for allegedly disclosing cationic peptides that fold into an amphipathic helical conformation having antimicrobial properties (Office Action, pp. 15-16). However, the peptides disclosed in Cascales lack the claimed turn sequence ((d)PPT) and do not self-assemble into a hydrogel. Instead, the peptides disclosed in Cascales are free diffusible molecules in solution.
Purpose of Cascales is to show that antibacterial peptides can also be used to treat fungal infections, as explained in the teachings of Cascales. Moreover, Veiga teaches a peptide which is identical to applicants elected species.
(iii) Applicants argue that Jaynes and Namgoong fail to compensate for the defects of Veiga and Cascales, as both Jaynes and Namgoong fail to disclose the claimed peptides capable of self-assembling into a hydrogel.
Purpose of Jaynes is to show that peptides having potent antimicrobial activity, such as amphipathic/amphiphilic peptides with cationic charges, can treat fungal biofilms.
Similarly, the purpose of Namgoog is to show that debridement can be done prior to applying antimicrobial to facilitate the wound becoming self-sustaining in terms of a positive wound-healing trajectory.
(iv) Applicants argue that referring specifically to claim 4 and new claim 83, the Examiner contends that Veiga discloses the use of the counterion acetate in the synthesis of the peptide (Office Action, pp. 16-17). The Examiner's contention is erroneous. Veiga discloses synthesis with trifluoroacetic acid (TFA) as the counterion (p. 3) - the standard residual from IPLC purification using TFA-containing mobile phases. Thus, Veiga is silent regarding any acetate counterion, and instead discloses a peptide having TFA.
Even if cited art does not teach counterions, but these are well known in the art. Skilled person in the art would incorporate suitable counter ions to make salt form to increase the solubility and stability of the peptide.
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 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.
(i) Claims 1, 4, 20, 50, 55, 66, 67, 69, 70, 75-77 and 80-84 are rejected under 35 U.S.C. 103 as being unpatentable over Veiga (Biomaterials vol. 33,35 (2012): 8907-16; see IDS filed 10/06/2023) in view of Cascales (ACS omega vol. 3,5 (2018): 5390-5398).
With regard to claim 1, Veiga teaches a method of treating bacterial infections comprising administering a preparation comprising hydrogels of self-assembling ß-hairpin peptides, including SEQ ID NO: 2 of the instant application, VKVRVRVRVPPTRVRVRVKV (PEP6R), an amphiphilic peptide (see Abstract, page 8912, paragraph 3). In antibacterial assays, they further teach using the peptides in an aqueous buffer, BTP, with water and sodium chloride (see page 8909, paragraph 8 and page 8910, paragraph 1), and they teach that all peptides were purified as a part of the peptide synthesis (see page 8908, paragraph 4).
Veiga does not teach that the method is drawn to administering an amount effective to promote deactivation of a target fungal organism associated with a fungal contamination. This can be cured from the teachings of Cascales, see below.
Cascales teaches that a great number of cationic peptides that are the first natural barrier against external pathogens have been discovered and characterized, and that two main characteristics of these cationic peptides are that they have positive charges, ranging from +2 to +9, and that they fold in an amphipathic helical conformation, with two well-defined hydrophilic and hydrophobic faces (see page 5390, paragraph 2). They further teach that, in line with the action mechanism of these antimicrobial peptides, there is a wide consensus that these peptides focus their target on the destabilization of the cell membrane of Gram-negative and Gram-positive bacteria and fungus (see page 5390, paragraph 4 and page 5391, paragraph 1). They argue that these peptides exert their lytic activity against pathogens by electrostatic interactions with the negative charge of the microbial cell surfaces (favored by the positive charge of these cationic peptides) and subsequent pathogen membrane disruption, meaning that the positive charge of the cationic peptide seems to be a crucial aspect that needs to be considered in the discrimination process between the pathogen and host cells (see page 5391, paragraph 1). In other words, the positive charge of these peptides, together with the amphipathic nature of their alpha helical conformation, seems to be key aspects for their antibacterial and antifungal activity, particularly for peptides with a charge less than or equal to +9 (see page 5391, paragraph 2). Given this, Cascales provide a clear motivation and explanation for why small, positively charged, amphiphilic peptides with antibacterial activity may also have antifungal activity. Specifically, they argue that the positive charge interacts with the cell membrane of bacterial or fungal pathogens. As such, they provide a clear motivation for the use of positively charged (less than or equal to +9) amphiphilic small peptides with antibacterial activity in treating fungal pathogens with a reasonable expectation of success. Here, Veiga explicitly teach that the net formal charge of PEP6R at neutral pH is +9 per monomer (see page 8912, paragraph 6). Given this clear motivation, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references of Cascales and Veiga to use the invention of Veiga to treat fungal contaminations.
With regard to claim 4, Veiga teaches the use of an acetate counterion, in the peptide synthesis, and they do not teach the use of chloride in any form in the synthesis of the peptide (see page 8908, paragraph 4). As such, they teach a peptide according to the claim limitations that does not have chloride counterions, seeing as chloride-containing compounds are not used in the peptide synthesis, and a different counterion, an acetate, is used.
With regard to claim 15, Cascales teach topical applications of the cationic and amphiphilic peptides because peptides that have negligible lethality and toxicity for mammalian cells in vitro have frequently been found to be toxic when they were injected into the bloodstream (see page 5391, paragraph 3). Given the motivation to combine the references of Veiga and Cascales discussed above, as well as the clear motivation to use topical administration for the cationic and amphiphilic peptides of Cascales, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references of Veiga and Cascales to use the method of Veiga with topical administration.
With regard to claim 20, as discussed above, Veiga teaches the peptide of SEQ ID NO: 2, VKVRVRVRVPPTRVRVRVKV, of the instant application (see Abstract), and this is the elected species that reads on claim 20 of the instant application. Here, products of identical chemical composition cannot have mutually exclusive properties (In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990)). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Therefore, the PEP6R inherently has the folding group, turn sequence, and residues recited in claim 20 of the instant application.
With regard to claim 50, Veiga teaches PEP6R gels prepared at 1.5 wt % or higher concentration, which demonstrated high antimicrobial activity (see Abstract). Beyond this, they teach that Aat 0.5 wt% the hydrogel surface of PEP2R shows minimal action, but as the wt% is increased, the gel surface gains activity in a wt%-dependent manner wherein 2 wt% gels inhibit proliferation of about 50% of the introduced bacteria as compared to about 10% in the 0.5 wt% gel (see page 8911, paragraph 2). Given the reasoning to combine the references recited above, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to use the method of Veiga to treat fungal infections. Although this range, roughly from 0.5% to 2% w/v, does not overlap exactly with the claimed range of 0.5% to 3.0% w/v, in the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) The prior art taught carbon monoxide concentrations of "about 1-5%" while the claim was limited to "more than 5%." The court held that "about 1-5%" allowed for concentrations slightly above 5% thus the ranges overlapped.); In re Geisler, 116 F.3d 1465, 1469-71, 43 USPQ2d 1362, 1365-66 (Fed. Cir. 1997) A claim reciting thickness of a protective layer as falling within a range of "50 to 100 Angstroms" was considered prima facie obvious in view of prior art reference teaching that "for suitable protection, the thickness of the protective layer should be not less than about 10 nm [i.e., 100 Angstroms]." Here, given that the ranges are nearly entirely overlapping, a case of obviousness exists.
With regard to claims 54 and 55, as discussed above, Veiga teach the peptide of SEQ ID NO: 2 of the instant application, VKVRVRVRVPPTRVRVRVKV (PEP6R) (see Abstract). Veiga teaches that the net formal charge of PEP6R at neutral pH is +9 per monomer (see page 8912, paragraph 6). Although this value, +9, does not entirely overlap with the claimed ranged +2 to +11 or +5 to +9, as discussed above, in the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) The prior art taught carbon monoxide concentrations of "about 1-5%" while the claim was limited to "more than 5%." The court held that "about 1-5%" allowed for concentrations slightly above 5% thus the ranges overlapped.); In re Geisler, 116 F.3d 1465, 1469-71, 43 USPQ2d 1362, 1365-66 (Fed. Cir. 1997) A claim reciting thickness of a protective layer as falling within a range of "50 to 100 Angstroms" was considered prima facie obvious in view of prior art reference teaching that "for suitable protection, the thickness of the protective layer should be not less than about 10 nm [i.e., 100 Angstroms]." Here, given that the peptide of SEQ ID NO: 2 falls within each range, a case of obviousness exists.
With regard to claim 66, Veiga teaches that hydrogel materials that display inherent activity against bacteria can be used to directly treat accessible wounds to prevent or kill existing infection, that hydrogels composed of self-assembling ß-hairpin peptides, having a high content of arginine, are extremely effective antimicrobials (see Abstract).
With regard to claim 67, as discussed above, Veiga teaches that hydrogel materials that display inherent activity against bacteria can be used to directly treat accessible wounds to prevent or kill existing infection, that hydrogels composed of self-assembling ß-hairpin peptides, having a high content of arginine, are extremely effective antimicrobials (see Abstract). They also teach that microbial infections are a common problem associated with dermal wounds, within which P. aeruginosa accounts for 10% of all hospital infections, and this is particularly relevant for patients with cancer, AIDS, burns, or cystic fibrosis (see page 8907, paragraph 1). Seeing as the hydrogels of the invention of Veiga are extremely effective against P. aeruginosa (see Abstract), there exists a clear motivation to use this hydrogel to treat the patients that Veiga identity as affected by P. aeruginosa, namely hospitalized patients with cancer, AIDS, burns, or cystic fibrosis (see Abstract and page 8907, paragraph 1). As such, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to use the hydrogels of Veiga to treat trauma wounds, specifically burns.
With regard to claim 69, Veiga teach the use of a buffer comprising 150 mM sodium chloride and 50 mM BTP (see page 8910, paragraph 1). They explicitly teach using this buffer along with the peptides directly in wells of tissue-culture treated plates to test its antimicrobial ability (see page 8910, paragraph 1). Here, the buffer is therefore used at the target site (see page 8910, paragraph 1). Moreover, Veiga teaches that the addition of buffer triggers peptide folding, self-assembly (see page 8910, paragraph 1).
With regard to claim 70, Veiga teaches the use of a buffer comprising 150 mM sodium chloride and 50 mM BTP (see page 8910, paragraph 1). As discussed above, in the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990) The prior art taught carbon monoxide concentrations of "about 1-5%" while the claim was limited to "more than 5%." The court held that "about 1-5%" allowed for concentrations slightly above 5% thus the ranges overlapped.); In re Geisler, 116 F.3d 1465, 1469-71, 43 USPQ2d 1362, 1365-66 (Fed. Cir. 1997) A claim reciting thickness of a protective layer as falling within a range of "50 to 100 Angstroms" was considered prima facie obvious in view of prior art reference teaching that "for suitable protection, the thickness of the protective layer should be not less than about 10 nm [i.e., 100 Angstroms]." Here, given that the value of Veiga falls within the range, a case of obviousness exists.
With regard to claims 75-77 and 80-81, Veiga teaches sequence VKVRVRVRVPPTRVRVRVKV (PEP6R), which is identical to applicants elected SEQ ID NO:2, and has six Arg (see Abstract, page 8912, paragraph 3).
With regard to claim 82, see With regard to claim 50, above. It appears that this claims is duplicate of claim 50.
With regard to claim 83, Veiga does not say anything about TFA in the purified peptide [see Supplementary Material], and this is interpreted as peptide is free from TFA.
With regard to claim 84, there is no acetylation on N-terminus of peptide in the teachings of Veiga [see abstract].
Motivation to combine the art can arise from the expectation that the prior art elements will perform their expected functions to achieve their expected results when combined for their common known purpose. See MPEP 2144.07. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention by taking the advantage of the teaching of the above cited reference and to make the instantly claimed method with a reasonable expectation of success.
A combination of prior art references is only proper if a person of ordinary skill in the art (POSA) at the time of the invention, faced with the same problem, would have been motivated to combine their teachings with a reasonable expectation of success. See KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398 (2007). Here, the technical fields and problems addressed by the references are not distinct from that of the present claimed invention.
The strongest rationale for combining references is a recognition, expressly or impliedly in the prior art or drawn from a convincing line of reasoning based on established scientific principles or legal precedent, that some advantage or expected beneficial result would have been produced by their combination. In re Sernaker, 702 F.2d 989, 994-95, 217 USPQ 1, 5-6 (Fed. Cir. 1983).
(ii) Claims 1, 4, 8-11, 20, 32, 36, 50, 55-57, 65-67, 69-70, 75-77 and 80-84 are rejected under 35 U.S.C. 103 as being unpatentable over Veiga (Biomaterials vol. 33,35 (2012): 8907-16; see IDS filed on 10/06/2023) in view of Cascales (ACS omega 2018, vol. 3,5: 5390-5398), as applied to claims 1, 20, 50, 55, 66, 67, 69, 70, 75-77 and 80-84 above and in further view of Jaynes (US 10,548,944 B1).
The teachings of Veiga and Cascales have been set forth above.
With regard to claim 8, Veiga additionally teaches the method of treating microbial infections using the hydrogels discussed above. Specifically, Veiga teaches a method of treating bacterial infections comprising administering a preparation comprising hydrogels of self-assembling ß-hairpin peptides, including SEQ ID NO: 2 of the instant application, VKVRVRVRVPPTRVRVRVKV (PEP6R), an amphiphilic peptide (see Abstract, page 8912, paragraph 3). They do not, however, teach that the method is drawn to administering an amount effective to promote deactivation of a target fungal organism associated with a fungal contamination. As discussed above, Cascales provide a clear motivation for using peptides like those used to form the hydrogel of Veiga in treating fungal contaminations. Neither reference, however, teaches treating biofilms.
Jaynes teaches peptides having potent antimicrobial activity, broad-spectrum antimicrobial activity, and/or the ability to kill otherwise antibiotic-resistant microbes, or microbes protected by biofilms (see Abstract). More specifically, they teach amphipathic/amphiphilic peptides with cationic charges, including +9 (see column 9, lines 36-40). They teach peptides with positive charges on their polar surface, including the peptide RP557, are capable of interacting with and disrupting the negatively charged phospholipids on the cell membranes of microorganisms (see column 35, lines 9-12). They further teach that the RP557 peptide, which is characterized as a short, amphiphilic/amphipathic, cationic peptide, prevents and treats biofilms of various bacterial and fungal species like Candida albicans found in wounds thereby mitigating the influence of infection on healing and regeneration (see column 35, lines 65-67, column 36, lines 1-3, and Fig. 5A to 5B). Here, Jaynes et al. provide a clear motivation for the use of small, cationic, amphiphilic peptides in treating fungal infections like Candida albicans because of the fact that the positive charges of the peptides interact with and disrupt the negatively charged phospholipids of the microorganism membrane. Beyond this, Jaynes et al. also provide a motivation for using hydrogel forms of the treatment because they represent a convenient topical ophthalmic delivery system (see column 26, lines 10-18). Given the motivations for using small, cationic, amphiphilic peptides with +9 charge in treating fungal infections, as well as the motivation for using the treatments of the invention of Jaynes in hydrogels, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references and use the method of Veiga to treat fungal biofilms.
With regard to claims 9 and 10, as discussed above, Jaynes teach peptides having potent antimicrobial activity, broad-spectrum antimicrobial activity, and/or the ability to kill otherwise antibiotic-resistant microbes, or microbes protected by biofilms (see Abstract). They teach peptides with positive charges on their polar surface, including the peptide RP557, are capable of interacting with and disrupting the negatively charged phospholipids on the cell membranes of microorganisms (see column 35, lines 9-12). They further teach that the RP557 peptide, which is characterized as a short, amphiphilic/amphipathic, cationic peptide, prevents and treats biofilms of various bacterial and fungal species like Candida albicans found in wounds thereby mitigating the influence of infection on healing and regeneration (see column 35, lines 65-67, column 36, lines 1-3, and Fig. 5A to 5B). Again, given the reasoning discussed above, it would have been obvious to combine the references of Jaynes and Veiga to use the method of Veiga in treating Candida albicans.
With regard to claim 11, Jaynes teaches that the subject peptide composition, alone or in combination with antibiotic and/or anti-inflammatory agents, is applied to burn wounds as a gel, ointment or cream, and/or administered systemically (see column 26, lines 64-67). Topical application can prevent systemic infection following superficial colonization or eradicate a superficial infection (see columns 26, line 67 and column 27, lines 1-2). In some cases, the subject composition can be administered as a 0.5% to 5% gel, cream, or ointment, such as 0.5 to 2%, as described herein, and application to the skin could be performed once a day or as often as dressings are changed (see column 27, lines 2-6). Here, Jaynes teaches topical application to the skin, an integumental tissue. Given the reasoning discussed above, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references of Jaynes and Veiga to use the method of Veiga in treating fungal infections according to the methods of Jaynes.
With regard to claim 32, Jaynes teach using the cationic amphiphilic peptides, specifically the peptide RP557 discussed above, at 98% purity or better (see column 35, lines 13-14). Again, given the reasoning provided above, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references.
With regard to claim 56, Jaynes teach that the composition is a lyophilized composition that can be provided to an end use in a solid form suitable for reconstitution with a liquid, e.g., an aqueous solution (see column 20, lines 41-44).
With regard to claim 57, Jaynes teach the compositions of their invention can function as sterilizing agents and can serve as sterile storage media (see column 23, lines 7-20).
With regard to claim 65, Jaynes teach treating fungal infections in rats, specifically vulvovaginal candidiasis caused by C. albicans (see column 36, lines 52-55 and column 2, lines 64-67).
(iii) Claims 1, 4, 8-11, 20, 32, 36, 50, 55-57, 62, 65-67, 69-70, 75-77 and 80-84 are rejected under 35 U.S.C. 103 as being unpatentable over Veiga (Biomaterials vol. 33,35 (2012): 8907-16; see IDS filed on 10/06/2023) in view of Cascales (ACS omega vol. 3,5 (2018): 5390-5398), as applied to claims 1, 20, 50, 55, 66, 67, 69, 70, 75-77 and 80-84 above and in further view of Jaynes (US 10,548,944 B1) and Namgoong (Journal of plastic surgery and hand surgery vol. 54,1 (2020): 47-54).
The teachings of Veiga, Cascales and Jaynes have been set forth above.
With regard to claim 62, Jaynes teaches that infection is the predominant determinant of wound healing, incidence of complications, and outcome of burn patients, and that frequent debridement’s and establishment of an epidermis or a surrogate, such as a graft or a skin substitute, significantly aids in the prevention of infection (see column 26, lines 57-63). Here, Jaynes provides a clear motivation for frequent debridement of a wound area on account of its ability to prevent infection. Moreover, they teach local topical application directly to wounds or areas in need of treatment (see column 22, lines 1-9). They also teach that the subject peptide composition, alone or in combination with antibiotic and/or anti-inflammatory agents, is applied to burn wounds as a gel, ointment or cream, and/or administered systemically (see column 26, lines 64-67). Although Jayneses clearly motivate debridement of the wound and application of the peptide composition directly to the wound area in need of treatment, they do not explicitly say that debridement is done prior to applying the antimicrobial composition. Here, Namgoong teaches that it is known in the art (i.e. in current treatment guidelines) that debridement is done prior to applying antimicrobials to facilitate the wound becoming self-sustaining in terms of a positive wound-healing trajectory (see Abstract). This provides a clear motivation to use debridement of the target area prior to applying antimicrobials, which facilitate the healing of the wound. Seeing as Jaynes teaches the use of debridement to prevent infection, and given this clear motivation from Namgoog it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references and perform debridement before applying the antimicrobials.
Nonstatutory Double Patenting Rejections
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.
(i) Claims 1, 4, 20, 50, 55, 69, 70, 75-77 and 80-84 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 42, 28, 46, 47, 55, 73, 77, and 83 of copending Application No. 18/682493 (hereinafter Mehta) in view of Veiga (Biomaterials vol. 33,35 (2012): 8907-16; see IDS filed 10/06/2023) and Cascales (ACS omega vol. 3,5 (2018): 5390-5398).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
With regard to claim 1, Mehta claims a method of treating a nerve injury, comprising: administering to a target site of a nerve injury a preparation comprising a purified amphiphilic peptide in an aqueous biocompatible solution, the peptide comprising a folding group having a plurality of charged amino acid residues and hydrophobic amino acid residues arranged in a substantially alternating pattern and a turn sequence, the peptide being configured to self-assemble into a hydrogel, in an amount effective to treat the nerve injury (see claim 1 of the reference application). Moreover, they claim that the folding group has a sequence comprising Y[XY]N[T][YX]MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10, and wherein the turn sequence amino acids are independently selected from a D-proline, an L- proline, aspartic acid, threonine, asparagine, and combinations thereof (see claims 46 and 47). This sequence includes SEQ ID NO: 2 of both the reference and the instant application, which the instant application elected as the peptide sequence for the hydrogel. Mehta does not, however, explicitly claim the use of the hydrogel with this sequence for treating fungal contamination.
As discussed above, Veiga teaches a method of treating bacterial infections comprising administering a preparation comprising hydrogels of self-assembling ß-hairpin peptides, similarly including SEQ ID NO: 2 of the instant application, VKVRVRVRVPPTRVRVRVKV (PEP6R), an amphiphilic peptide (see Abstract, page 8912, paragraph 3). In antibacterial assays, they further teach using the peptides in an aqueous buffer, BTP, with water and sodium chloride (see page 8909, paragraph 8 and page 8910, paragraph 1), and they teach that all peptides were purified as a part of the peptide synthesis (see page 8908, paragraph 4). Here, provides a clear motivation for using the peptide of the hydrogel of Mehta in treating microbial infections, particularly bacterial infections. As such, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to use the method of Mehta in treating bacterial infections. Again, Veiga does not teach that the method is drawn to administering an amount effective to promote deactivation of a target fungal organism associated with a fungal contamination.
Cascales teach that a great number of cationic peptides that are the first natural barrier against external pathogens have been discovered and characterized, and that two main characteristics of these cationic peptides are that they have positive charges, ranging from +2 to +9, and that they fold in an amphipathic helical conformation, with two well-defined hydrophilic and hydrophobic faces (see page 5390, paragraph 2). They further teach that, in line with the action mechanism of these antimicrobial peptides, there is a wide consensus that these peptides focus their target on the destabilization of the cell membrane of Gram-negative and Gram-positive bacteria and fungus (see page 5390, paragraph 4 and page 5391, paragraph 1). They argue that these peptides exert their lytic activity against pathogens by electrostatic interactions with the negative charge of the microbial cell surfaces (favored by the positive charge of these cationic peptides) and subsequent pathogen membrane disruption, meaning that the positive charge of the cationic peptide seems to be a crucial aspect that needs to be considered in the discrimination process between the pathogen and host cells (see page 5391, paragraph 1). In other words, the positive charge of these peptides, together with the amphipathic nature of their alpha helical conformation, seems to be key aspects for their antibacterial and antifungal activity, particularly for peptides with a charge less than or equal to +9 (see page 5391, paragraph 2). Given this, Cascales provide a clear motivation and explanation for why small, positively charged, amphiphilic peptides with antibacterial activity may also have antifungal activity. Specifically, they argue that the positive charge interacts with the cell membrane of bacterial or fungal pathogens. As such, they provide a clear motivation for the use of positively charged (less than or equal to +9) amphiphilic small peptides with antibacterial activity in treating fungal pathogens with a reasonable expectation of success. Here, Veiga explicitly teach that the net formal charge of PEP6R at neutral pH is +9 per monomer (see page 8912, paragraph 6), and Mehta teach the same peptide as that of Veiga, as discussed above (see claims 46 and 47). Given this clear motivation, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references of Cascales, Veiga and Mehta to use the peptides of Veiga and Mehta to treat fungal contaminations.
With regard to claim 4, Mehta claim the method discussed above wherein the peptide comprises an effective amount of acetate, citrate, and/or chloride counterions (see claims 39, 4, and 41), and that the peptide is substantially free of chloride counterions. Given that the counterions are claimed in the alternative, the claims clearly include embodiments wherein the counterions are acetate or citrate and not chloride.
With regard to claims 8-10, as discussed above, Mehta claim the method discussed above wherein the folding group has a sequence comprising Y[XY]N[T][YX]MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10, and wherein the turn sequence amino acids are independently selected from a D-proline, an L- proline, aspartic acid, threonine, asparagine, and combinations thereof (see claims 46 and 47). This sequence includes SEQ ID NO: 2 of both the reference and the instant application, which the instant application elected as the peptide sequence for the hydrogel. Although Mehta do not explicitly claim the use of the hydrogel with this sequence for treating fungal contamination, “products of identical chemical composition cannot have mutually exclusive properties" (In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990)). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Moreover, "the discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer" (Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999)). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable (In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977)). Here, applying the method of Mehta to treating a different target organism because of the discovery of an unappreciated property in treating fungal organisms does not make the claim patentable.
With regard to claim 11, Mehta claim treating nervous tissue (see claim 3).
With regard to claim 15, Mehta claim topical, parenteral, and enteral administration (see claim 28).
With regard to claim 20, Mehta claim the method discussed above wherein: the hydrophobic amino acid residues are independently selected from glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, threonine, tryptophan, and combinations thereof; and the charged amino acid residues are independently selected from arginine, lysine, histidine, and combinations thereof (see claim 46). They further claim the method wherein the folding group has a sequence comprising Y[XY]N[T][YX]MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10, and wherein the turn sequence amino acids are independently selected from a D-proline, an L- proline, aspartic acid, threonine, asparagine, and combinations thereof (see claim 47).
With regard to claim 32, Mehta claim the method discussed above wherein the peptide is at least 80% purified (see claim 55).
With regard to claim 50, Mehta claim the method discussed above wherein the preparation comprises between 0.1% w/v and 8.0% w/v of the peptide (see claim 73). Although this is range is not identical to the claimed range of the instant application, "a prior art reference that discloses a range encompassing a somewhat narrower claimed range is sufficient to establish a prima facie case of obviousness" (In re Peterson, 315 F.3d 1325, 1330, 65 USPQ2d 1379, 1382-83 (Fed. Cir. 2003). See also In re Harris, 409 F.3d 1339, 74 USPQ2d 1951 (Fed. Cir. 2005) (claimed alloy held obvious over prior art alloy that taught ranges of weight percentages overlapping, and in most instances completely encompassing, claimed ranges; furthermore, narrower ranges taught by reference overlapped all but one range in claimed invention). Here, the range of Mehta encompasses the claim of the instant application and is not so broad as to encompass a very large number of possible distinct compositions.
With regard to claim 55, Mehta claim the method discussed above wherein the peptide is cationic or anionic, the cationic peptide having a net charge of from +2 to +11 (see claim 77). Again, although this is range is not identical to the claimed range of the instant application, "a prior art reference that discloses a range encompassing a somewhat narrower claimed range is sufficient to establish a prima facie case of obviousness" (In re Peterson, 315 F.3d 1325, 1330, 65 USPQ2d 1379, 1382-83 (Fed. Cir. 2003). See also In re Harris, 409 F.3d 1339, 74 USPQ2d 1951 (Fed. Cir. 2005) (claimed alloy held obvious over prior art alloy that taught ranges of weight percentages overlapping, and in most instances completely encompassing, claimed ranges; furthermore, narrower ranges taught by reference overlapped all but one range in claimed invention). Here, the range of Mehta encompasses the claim of the instant application and is not so broad as to encompass a very large number of possible distinct compositions.
With regard to claim 57, Mehta claims the method discussed above wherein the preparation is sterilized by autoclave sterilization (see claim 83).
With regard to claim 65, as discussed above, Mehta claims a method of treating a nerve injury, comprising: administering to a target site of a nerve injury a preparation comprising a purified amphiphilic peptide in an aqueous biocompatible solution, the peptide comprising a folding group having a plurality of charged amino acid residues and hydrophobic amino acid residues arranged in a substantially alternating pattern and a turn sequence, the peptide being configured to self-assemble into a hydrogel, in an amount effective to treat the nerve injury (see claim 1 of the reference application). Moreover, they claim that the folding group has a sequence comprising Y[XY]N[T][YX]MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10, and wherein the turn sequence amino acids are independently selected from a D-proline, an L- proline, aspartic acid, threonine, asparagine, and combinations thereof (see claims 46 and 47). This sequence includes SEQ ID NO: 2 of both the reference and the instant application, which the instant application elected as the peptide sequence for the hydrogel. Although Mehta do not explicitly claim the use of the hydrogel with this sequence for treating fungal contamination, “products of identical chemical composition cannot have mutually exclusive properties" (In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990)). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Moreover, "the discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer" (Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999)). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable (In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977)).
With regard to claims 69 and 70, Mehta claims the method discussed above, further comprising administering to the target site a buffer comprising an effective amount of an ionic salt and a biological buffering agent to form the hydrogel, wherein the buffer comprises between about 10 mM and 150 mM sodium chloride and between about 10 mM and 100 mM Bis-tris propane (BTP) (see claim 42).
With regard to claims 75-77 and 80-81, see With regard to claim 1 above.
With regard to claim 82, see With regard to claim 50 above.
With regard to claim 83, Mehta does not say anything about TFA in the purified peptide, and this is interpreted as peptide is free from TFA.
With regard to claim 84, there is no acetylation on N-terminus of peptide in the teachings of Mehta.
(ii) Claims 1, 4, 8-11, 20, 32, 36, 50, 55-57, 62, 65-67, 69-70, 75-77 and 80-84 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 7, 10, 14, 19, 31, 49, 53-56, 61, 64-66, and 68-69 of copending Application No. 18/040388 (hereinafter Kumar) in view of Veiga (Biomaterials vol. 33,35 (2012): 8907-16; see IDS filed 10/06/2023) and Cascales (ACS omega vol. 3,5 (2018): 5390-5398).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
With regard to claim 1, Kumar claim a method of treating a microbial contamination associated with a community of microorganisms of a subject in need thereof, comprising administering to a target site of the subject a thermally stable preparation comprising a purified amphiphilic peptide in an aqueous biocompatible solution, the peptide comprising a folding group having a plurality of charged amino acid residues and hydrophobic amino acid residues arranged in a substantially alternating pattern and a turn sequence, the peptide being configured to self-assemble into a hydrogel, in an amount effective to promote deactivation of a target microorganism associated with the microbial contamination (see claim 1). Kumar claim the method discussed above wherein the folding group has a sequence comprising Y[XYlN[T][YX1MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10;the hydrophobic amino acid residues are independently selected from glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, threonine, tryptophan, and combinations thereof; and the charged amino acid residues are independently selected from arginine, lysine, histidine, and combinations thereof, and the turn sequence amino acids are independently selected from a D-proline, an L-proline, aspartic acid, threonine, asparagine, and combinations thereof (see claim 19). This sequence includes SEQ ID NO: 2 of both the reference and the instant application, VKVRVRVRVPPTRVRVRVKV (PEP6R), which the instant application elected as the peptide sequence for the hydrogel. Kumar does not, however, explicitly claim the use of the hydrogel with this sequence for treating fungal contamination.
Cascales teaches that a great number of cationic peptides that are the first natural barrier against external pathogens have been discovered and characterized, and that two main characteristics of these cationic peptides are that they have positive charges, ranging from +2 to +9, and that they fold in an amphipathic helical conformation, with two well-defined hydrophilic and hydrophobic faces (see page 5390, paragraph 2). They further teach that, in line with the action mechanism of these antimicrobial peptides, there is a wide consensus that these peptides focus their target on the destabilization of the cell membrane of Gram-negative and Gram-positive bacteria and fungus (see page 5390, paragraph 4 and page 5391, paragraph 1). They argue that these peptides exert their lytic activity against pathogens by electrostatic interactions with the negative charge of the microbial cell surfaces (favored by the positive charge of these cationic peptides) and subsequent pathogen membrane disruption, meaning that the positive charge of the cationic peptide seems to be a crucial aspect that needs to be considered in the discrimination process between the pathogen and host cells (see page 5391, paragraph 1). In other words, the positive charge of these peptides, together with the amphipathic nature of their alpha helical conformation, seems to be key aspects for their antibacterial and antifungal activity, particularly for peptides with a charge less than or equal to +9 (see page 5391, paragraph 2). Given this, Cascales provides a clear motivation and explanation for why small, positively charged, amphiphilic peptides with antibacterial activity may also have antifungal activity. Specifically, they argue that the positive charge interacts with the cell membrane of bacterial or fungal pathogens. As such, they provide a clear motivation for the use of positively charged (less than or equal to +9) amphiphilic small peptides with antibacterial activity in treating fungal pathogens with a reasonable expectation of success. Here, Kumar explicitly teaches that the net formal charge their peptides at neutral pH are between +5 and +9 (see claim 54). Given this clear motivation, it would have been obvious to one having ordinary skill in the art prior to the effective filing date of the instant application to combine the references of Cascales and Kumar to use the peptides of Kumar to treat fungal contaminations with a reasonable expectation of success.
With regard to claim 4, Kumar claim the method discussed above wherein the peptide chloride counterions and the counterions selected from acetate and citrate counterions (see claim 4).
With regard to claims 8-10, as discussed above, Kumar claims a method of treating a microbial contamination associated with a community of microorganisms of a subject in need thereof, comprising administering to a target site of the subject a thermally stable preparation comprising a purified amphiphilic peptide in an aqueous biocompatible solution, the peptide comprising a folding group having a plurality of charged amino acid residues and hydrophobic amino acid residues arranged in a substantially alternating pattern and a turn sequence, the peptide being configured to self-assemble into a hydrogel, in an amount effective to promote deactivation of a target microorganism associated with the microbial contamination (see claim 1). Kumar claims the method discussed above wherein the folding group has a sequence comprising Y[XYlN[T][YX1MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10;the hydrophobic amino acid residues are independently selected from glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, threonine, tryptophan, and combinations thereof; and the charged amino acid residues are independently selected from arginine, lysine, histidine, and combinations thereof, and the turn sequence amino acids are independently selected from a D-proline, an L-proline, aspartic acid, threonine, asparagine, and combinations thereof (see claim 19). This sequence includes SEQ ID NO: 2 of both the reference and the instant application, which the instant application elected as the peptide sequence for the hydrogel. Although Mehta do not explicitly claim the use of the hydrogel with this sequence for treating fungal contamination, “products of identical chemical composition cannot have mutually exclusive properties" (In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990)). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Moreover, "the discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer" (Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999)). Thus, the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable (In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977)). Here, applying a method of microbial infections broadly to treating pathogenic C. albicans fungal infections or biofilms does not make the method patentable.
With regard to claim 11, Kumar claim the method discussed above wherein the target site is a tissue selected from mesenchymal tissue, connective tissue, muscle tissue, nervous tissue, embryonic tissue, dermal tissue, bone tissue, dental tissue, corneal tissue, cutaneous tissue, integumental tissue, soft tissue, and hard tissue, or a biological fluid selected from tears, mucus, urine, menses, blood, wound exudates, and mixtures thereof (see claim 10).
With regard to claim 20, Kumar claims the method discussed above wherein the folding group has a sequence comprising Y[XYlN[T][YX1MY, where X is 1-3 charged amino acids, Y is 1-3 hydrophobic amino acids, T is 2-8 turn sequence amino acids, and N and M are each independently between 2 and 10;the hydrophobic amino acid residues are independently selected from glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, threonine, tryptophan, and combinations thereof; and the charged amino acid residues are independently selected from arginine, lysine, histidine, and combinations thereof, and the turn sequence amino acids are independently selected from a D-proline, an L-proline, aspartic acid, threonine, asparagine, and combinations thereof (see claim 19).
With regard to claim 32, Kumar claims the method discussed above wherein the peptide is at least 80% purified (see claim 31).
With regard to claim 50, Kumar claims the method discussed above wherein the preparation comprises between 0.5% w/v and 3.0% w/v of the peptide (see claim 49).
With regard to claim 55, Kumar claims the method discussed above wherein the peptide has a net charge of from +5 to +9 (see claim 54).
With regard to claim 56, Kumar claims the method discussed above wherein the peptide is lyophilized (see claim 55).
With regard to claim 57, Kumar claims the method discussed above wherein the preparation is sterile (see claim 56).
With regard to claim 62, Kumar claims the method discussed above further comprising debridement of the target tissue prior to administration of the preparation (see claim 61).
With regard to claim 65, Kumar claims the method discussed above wherein the microbial contamination is a microbial colonization or infection (see claim 64).
With regard to claim 66, Kumar claims the method discussed above wherein the target site is associated with a wound (see claim 65).
With regard to claim 67, Kumar claims the method discussed above comprising administering the preparation in an amount effective to treat at least one of partial and full thickness wounds (e.g., pressure sores, leg ulcers, diabetic ulcers), first and second degree burns, tunneled/undermined wounds, surgical wounds (e.g., associated with donor sites/grafts, tissue and cell grafts, Post-Moh's surgery, post laser surgery, podiatric, sound dehiscence), trauma wounds (e.g., abrasions, lacerations, burns, skin tears), gastrointestinal wounds (e.g., anal fistulas, diverticulitis, ulcers), and draining wounds (see claim 66).
With regard to claim 69, Kumar claims the method discussed above further comprising administering to the target site a buffer configured to induce self-assembly of the hydrogel (see claim 68).
With regard to claim 70, Kumar claims the method discussed above wherein the buffer comprises between about 10 mM and 150 mM sodium chloride and between about 10 mM and 100 mM Bis-tris propane (BTP) (see claim 69).
With regard to claims 75-77 and 80-81, see With regard to claim 1 above.
With regard to claim 82, see With regard to claim 50 above.
With regard to claim 83, Kumar does not say anything about TFA in the purified peptide, and this is interpreted as peptide is free from TFA.
With regard to claim 84, there is no acetylation on N-terminus of peptide in the teachings of Kumar.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/SUDHAKAR KATAKAM/Primary Examiner, Art Unit 1658
