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 .
DETAILED ACTION
The amendment to the claims filed after non-final office action on February 13, 2026 is acknowledged. Claims 15-16, 18, 26-27 were amended, claims 3-5, 8-9, 11, 13, 19-25, 28-33 were canceled and claims 1-2, 6-7, 10, 12, 14-18, 26-27 are pending in the instant application. The restriction was deemed proper and made final previous office action.
Claims 1-2, 6-7, 10, 12, 14 are withdrawn as being drawn to a non-elected species/invention. Claims 15-18 and 26-27 are examined on the merits of this office action.
Withdrawn Rejections/Objections
The objection of claims 15-16, 19 and 24 are withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claims 15-19, 22, 24, 26-29 and 33 under 35 U.S.C. 101 because the claimed invention is not directed to patent eligible subject matter is withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claims 15-19, 22, 24, 26-29 and 33 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claims 22 and 29 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or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention is withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claim(s) 15-19, 22, 24, 26-29, 33 under 35 U.S.C. 102(a)(1) as being anticipated by Beliveau (WO2008046228) is withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claims 18-19, 22, 24, 26, 28-29, 33 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, scope of enablement is withdrawn in view of amendment of the claims filed February 13, 2026.
The rejection of claims 15-19, 22, 24, 26-29 and 33 on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 of U.S. Patent No. 8058227 B2 is withdrawn in view of amendment of the claims filed February 13, 2026.
Declaration under 37 C.F.R. 1.132
The Declaration under 37 CFR 1.132 filed February 13, 2026 is sufficient to overcome the rejection of claims 18-19, 22, 24, 26, 28-29, 33 based upon 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, scope of enablement.
The Hoffman Declaration under 37 CFR 1.132 provides extensive experimental data demonstrating that the modified CSD peptides, particularly W94-101 (SEQ ID NO:8), are effective across multiple fibrosis related disease models, including lung fibrosis, skin fibrosis, heart failure/cardiac fibrosis, kidney fibrosis/failure, albuminuria and microvascular leakage. The declaration includes treatment protocols, multiple peptide embodiments (SEQ ID Nos:5-8), oral and subcutaneous administration data, and comparisons to approved fibrosis therapeutics. The declaration substantially overcomes the enablement rejection because it provides numerous working examples across multiple disease systems and routes of administration, demonstrates operative embodiments within the claimed scope, and supplies sufficient guidance such that a person of ordinary skill in the art could practice the claimed invention without undue experimentation. Although the declaration does not provide direct experimental evidence for every recited diseases, such as hypertension or interstitial lung disease, the declaration nevertheless provides substantial representative data across multiple fibrosis related and cardiovascular disease models sufficient to demonstrate possession and enabled of the claimed invention.
Maintained/Revised Rejection
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.
Claim(s) 15-18, 26-27 are/remain rejected under 35 U.S.C. 103 as being unpatentable over Beliveau (WO2008046228, cited previously) in view of Paraskevopoulou (Microorganisms 2018 May 23;6(2):47, cited previously) and Hong (Biochemical Pharmacology, Vol. 58, pp. 1775–1780, 1999, cited previously).
Regarding claim 15, Beliveau teaches a peptide comprising the sequence VTKYWFYR (see claims 1 and 7) which is identical to amino acids 3-10 of SEQ ID NO:8 (same core sequence without terminal lysines). Regarding claims 16-17, Beliveau teaches compositions comprising said peptide and an acceptable pharmaceutical carrier (see claims 1, 7, 12). Beliveau teaches a peptide comprising the sequence VTKYWFYR (see claims 1 and 7) which is identical to amino acids 94-101 of instant SEQ ID NO:4 and amino acids 3-10 of SEQ ID NO:8.
Beliveau is silent to the elected species of SEQ ID NO:8 which is VTKYWFYR with two terminal D-lysine residues (N- and C-terminal).
Paraskevopoulou teaches “Since the first reference of a polylysine tag as a protein solubilizing peptide tag in 1994, many studies (reviewed here) have investigated the effect of different peptide tags on protein expression and solubility, without affecting the proteins’ function and activity. In this original study, a formerly chemically synthesized protein of low solubility, the minibody, was instead expressed in E. coli with a 3-lysine tag incorporated in either the N- or the C-terminus. As a result, the aqueous solubility of the tagged protein was increased by a 100-fold” (see section 4.1). Paraskevopoulou teaches of introduction of two terminal charged lysine residues increased stability via inhibiting proteolytical degradation (see section 4.1, second paragraph, see also Table 2). Thus, clearly the addition of positively charged lysine residues to terminal ends are routine and know in the art for enhancing stability and solubility.
Hong teaches “an enantiomer may not be suitable as a therapeutic agent because its extremely long half-life may increase the side-effects. An alternative method to overcome this limitation is to replace the amino acid in the most susceptible site with a D-amino acid” (see introduction, right column first paragraph). “D-amino acid substitution(s) at both termini of the membrane-active peptide, which maintained the a-helical structure and the antimicrobial activity, improved the stability of peptides in the presence of serum. Interestingly, the diastereomers with D-amino acid in their termini had more improved activity in the presence of heat inactivated serum than KSLK and its enantiomer. These results suggested that partial D-amino acid substitutions of membrane-active peptide can improve the in vivo activity” (see Conclusion paragraph, last page). Substitution of terminal amino acids with D-amino acids are known in the art for improving stability.
It would have been obvious before the effective filing date of the claimed invention to modify the peptide of Beliveau by adding terminal lysine residues and substituting with D-amino acid lysines as taught by Paraskevopoulou and Hong. Paraskevopoulou teaches that introduction of terminal positively charged lysine residues enhances peptide solubility and stability. Hong further teaches that substitution of terminal amino acids with D-amino acids improve serum stability.
One of ordinary skill in the art would have been motivated to combine these teachings in order to improve the stability and half-life of Beliveau’s peptide while retaining biological activity, with a reasonable expectation of success, since both modifications are well known strategies in the peptide field for enhancing protease resistance, solubility and bioavailability.
Regarding claims 18 and 26, recitation that the composition or peptide is “for treating” a disease (e.g., microvascular leakage, CGF, scleroderma, skin fibrosis, etc…) is considered and intended use or statement of purpose, which does not further limit the claimed composition. A recitation of the intended use of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the intended use, then it meets the claim limitation. In the instant case, Beliveau in view of Paraskevopoulou and Hong teaches the same peptide of the instant claims thus, it would inherently possess the same properties and thus would be capable of performing the intended use as claimed.
Regarding claim 27, Beliveau teaches formulations for intraperitoneal and subcutaneous administration (see page 36, lines 5-12).
Response to Applicant’s Arguments
Applicant disagrees for at least the following reasons. Based on the combination of references set forth by the Examiner, Applicants assert that the rejection of the claims under § 103 could only have been made with hindsight bias and ex post reasoning. When applying 35 U.S.C. § 103, the following tenets of patent law must be followed: 1) the claimed invention must be considered as a whole; 2) the references must be considered as a whole; 3) the references must be viewed without the benefit of impermissible
hindsight vision afforded by the claimed invention; and 4) reasonable expectation of success is the standard with which obviousness is determined (MPEP § 2141 II). Establishing a prima facie case of obviousness of a claimed invention "requires a suggestion of all limitations in a claim" in the prior art. 35 U.S.C. § 103(a); CFMT, Inc. v. Yieldup Intern. Corp., 349 F.3d 1333, 1342 (Fed. Cir. 2003) (citing In re Royka, 490 F.2d 981, 985 (CCPA 1974); see also In re Ochiai, 71 F.3d 1565, 1572 (Fed. Cir. 1995). Therefore, in order to render claims 15-19, 22, 24, 26-29 and 33 obvious under 35 U.S.C. § 103, the combination of Beliveau, Paraskevopoulou and Hong must teach or suggest each and every element of the claims. To establish a prima facie case of obviousness, a reference or combination of references must: (1) suggest to those of ordinary skill in the art that they should make the claimed invention, and (2) reveal to those of ordinary skill in the art that they would have a reasonable expectation of success. In re Vaeck, 20 USPQ2d 1438, 1442 (Fed. Cir. 1991). Both the suggestion and the reasonable expectation of success must be found in the prior art and not in the Applicant's disclosure. In re Dow Chemical Company, 5 USPQ2d 1529, 1531 (Fed. Cir. 1988). However, there is nothing in any of the cited references that would motivate one of ordinary skill in the art to combine the teachings of these references to produce the presently claimed invention. Moreover, there is nothing in any of the cited references that would provide one of ordinary skill in the art with a reasonable expectation of success in making the combination in the presently claimed invention. "Reasonable expectation of success" is premised on predictability. In other words, to have a reasonable expectation of success, the ordinarily skilled artisan must be able to predict the likely outcome for an experiment. A direct corollary of this fact is that if one cannot predict the likely outcome for an experiment, one cannot have a reasonable expectation of success in achieving a given outcome. Indeed, the USPTO clearly recognizes the relationship between predictability and reasonable expectation of success. Specifically, MPEP 2143E articulates how to determine if a claim can be rejected on an "obvious-to-try" rationale using the following language:
As described above, claims 19, 22, 24, 28, 29 and 33 have been canceled herein, rendering the rejection of these claims moot. Without necessarily agreeing with the Office Action, but in an earnest effort to advance prosecution, Applicant has amended claim 15, upon which claims 16-18, 26 and 27 depend, to recite that the amino acid sequence is selected from the group consisting of SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8. As described above, Applicant submits that Beliveau does not teach or suggest a composition comprising the amino acid sequence is selected from the group consisting of SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8, much less provide evidence that the CSD peptide has increased solubility and stability in water, or the use of the water soluble CSD peptides for the treatment of fibrosis, microvascular leakage, congestive heart failure, scleroderma skin disease, skin fibrosis, interstitial lung diseases, renal inflammatory injury, kidney dysfunction, chronic kidney failure, or heart disease as claimed. Rather, Beliveau provides a laundry list of over 150 peptides from caveolin-1, but only demonstrates an effect with 2 peptides, neither of which is a modified peptide. Applicant submits that the novel modification making CSD and its three subregions water-soluble also improves their uptake into cells, their ability to inhibit kinases, and is likely to protect them from proteolysis. Applicant submits that the unmodified CSD peptides are only marginally soluble in water and have to be solubilized in DMSO. In previous studies, the oral delivery of peptide drugs was considered to be a challenge. Applicant submits that the modification making CSD- related peptides water soluble makes drug development studies, particularly for oral delivery, practical. A skilled artisan would not try to develop a peptide for oral delivery that required DMSO for solubilization. Applicant further submits that the invention is based, in part, on the development of SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8 which were specifically modified to increase the solubility in water, a pharmaceutically acceptable solute. The modification making CSD-related peptides water soluble makes drug development studies for oral delivery practical. Data provided in the accompanying Declaration demonstrates that W94-101 (SEQ ID NO:8) is effective when delivered orally, which is not predictable based on the cited references. The data provided in the Declaration further demonstrates that in side by side comparisons, W94-101 (SEQ ID NO:8) is more effective than existing drugs (Ofev, Esbriet) for lung fibrosis. The disclosures of Paraskevopoulou and Hong do not cure the deficiencies of Beliveau as they provide methods by which a multitude of differently modified sequences may be obtained, but does not teach or suggest the specific modified CSD sequences of SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8, much less provide any expectation that W94-101 (SEQ ID NO:8) would be effective when delivered orally or be more effective than Ofev and Esbriet for lung fibrosis. Applicants submit that the combination of Beliveau, Paraskevopoulou and Hong does not meet the requirements as set forth in MPEP 2143E that there were a finite number of identified, predictable potential solutions much less provide evidence that one of ordinary skill in the art could have pursued the known potential solutions with a reasonable expectation of success. Applicant submits that even using the methods of increasing protein stability of Paraskevopoulou and Hong, as suggested by the Office Action, there is still an open-ended genus of modified peptides that can be formed including peptides which may be modified to the extent that they have lost their functionality. A person of skill in the art having the ability to select any modification or combination thereof from the multiple modifications of Paraskevopoulou and Hong and the starting sequence of Beliveau would generate an unknown number of potential modified alternative peptides, which does not demonstrate that there were a finite number of identified, predictable modified peptide sequences. Applicants submit therefore that, contrary to the assertions of the Office Action, a person of skill in the art, provided with the combination of Beliveau, Paraskevopoulou and Hong, would still have had to select and apply the appropriate modifications and test the modifications to demonstrate that the modified peptides retained the appropriate activity to arrive at the peptides of SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8. Applicant submits that those of skill in the art would not have been lead directly to the peptides as set forth in SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8 as recited in claim 15, upon which claims 16-18, 26 and 27, but would have required an unacceptable level of experimentation to select the appropriate modifications to employ to arrive at SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8 from the starting sequence of Beliveau.
For at least the foregoing reasons, Applicant respectfully requests reconsideration and withdrawal of the rejection of claims 15-18, 26 and 27 under 35 U.S.C. § 103.
Applicant’s arguments have been fully considered but are not persuasive for the following reasons.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). However, the rejection is based on the express teachings of the cited references and a rational motivation to combine the references consistent with KSR. Beliveau teaches the base caveolin-1 scaffold domain peptide sequence, Paraskevopoulou teaches the addition of terminal positively charged lysine residues improves peptide solubility and stability, and Hong teaches that substitution of terminal amino acids with D amino acids improves serum stability and in vivo activity. One of ordinary skill in the art would have been motivated to apply these known peptide optimization strategies to Beliveau’s peptide in order to improve solubility, stability and bioavailability while retaining biological activity, with a reasonable expectation of success.
Applicant argues that the cited references do not teach or suggest SEQ ID Nos:5-8 specifically. However, obviousness does not require an express teaching of the exact claimed sequence. The proper inquiry is whether the claimed subject matter as a whole would have been obvious to one of ordinary skill in the art. Here, the cited references teach the starting peptide sequence and further teach the exact types of modifications recited in the claims, namely terminal lysine additions and terminal D-amino acid substitutions for improving peptide properties.
Applicant argues that there is no reasonable expectation of success and that peptide modification is unpredictable. This argument is not persuasive because both Paraskevopoulou and Hong expressly teach that the claimed modifications improve peptide solubility, stability, protease resistance, and/or in vivo activity. The rejection does not rely on random or unexplored modifications, but rather on known and routine peptide optimization strategies recognized in the art for achieving the same desired properties alleged by Applicant. Furthermore, MPEP2143.02 states “Conclusive proof of efficacy is not required to show a reasonable expectation of success. OSI Pharm., LLC v. Apotex Inc., 939 F.3d 1375, 1385, 2019 USPQ2d 379681 (Fed. Cir. 2019) ("To be clear, we do not hold today that efficacy data is always required for a reasonable expectation of success. Nor are we requiring ‘absolute predictability of success.’"); Acorda Therapeutics, Inc. v. Roxane Lab., Inc., 903 F.3d 1310, 1333, 128 USPQ2d 1001, 1018 (Fed. Cir. 2018) ("This court has long rejected a requirement of ‘[c]onclusive proof of efficacy’ for obviousness." (citing to Hoffmann-La Roche Inc. v. Apotex Inc., 748 F.3d 1326, 1331 (Fed. Cir. 2014); PharmaStem Therapeutics, Inc. v. ViaCell, Inc., 491 F.3d 1342, 1364 (Fed. Cir. 2007); Pfizer, Inc. v. Apotex, Inc., 480 F.3d 1348, 1364, 1367–68 (Fed. Cir. 2007) (reasoning that "the expectation of success need only be reasonable, not absolute"))”.
Applicant further argues that there was not a finite number of identified, predictable solutions and that numerous potential modified peptides could be generated. However, obviousness does not require that only a single possible modification exist. The cited references specifically direct one of ordinary skill in the art toward terminal lysine modification and terminal D amino acid substitution as recognized methods for improving peptide stability and solubility. Routine optimization among known options does not render the claimed invention non obvious.
Applicant argues that Beliveau only demonstrates activity for unmodified peptides and does not teach water soluble modified peptides or oral delivery. However, Paraskevopoulou expressly teaches that terminal lysine modifications increase solubility, while Hong teaches that terminal D amino acid substitutions improve stability in biological systems. Accordingly, the combination of references reasonably suggests modified peptides with improved pharmaceutical properties, including improved suitability for in vivo administration.
Applicant additionally relies upon the Declaration filed February 13, 2026 to argue that W94-101 demonstrates oral activity and superior efficacy relative to Ofev and Esbriet. The Declaration evidence has been considered but is not sufficient to overcome the prima facie case of obviousness. Evidence that the modified peptide exhibits beneficial properties does not outweigh the strong evidence that the claimed modifications themselves were known in the art for improving peptide solubility, stability, and in vivo performance.
Applicant additionally relies upon the Declaration data to assert that the claimed modified peptides possess unexpected properties and therefore unobvious. However, the data are not persuasive of unexpected results sufficient to overcome the prima facie case of obviousness. As acknowledged by Applicant, the core caveolin scaffold domain peptide sequence was already known in the art from Beliveau. Thus, the relevant inquiry is not whether the base peptide exhibits biological activity, but rather whether the specific modifications recited in the claims, namely terminal lysine additions and terminal D amino acid substitutions, resulted in properties that would have been unexpected to one of ordinary skill in the art.
The cited prior art expressly teaches that addition of terminal lysine residues enhances aqueous solubility and stability (Paraskevopoulou) and that substitution with terminal D-amino acids improves serum stability and in vivo activity (Hong). Accordingly, improvements in solubility, stability, protease resistance, and pharmaceutical utility would have been expected results of applying the known modifications taught by the art.
The Declaration does not provide comparative evidence demonstrating that the claimed modifications impart unexpectedly superior properties relative to the closest prior art peptide. In particular, Applicant does not provide side by side comparative data between the claimed modified peptides and the corresponding unmodified Beliveau peptide under equivalent conditions sufficient to establish that the observed biological activity or oral efficacy arises form an unexpected property attributable to the claimed lysine and D-amino acid modifications themselves.
Rather, the Declaration largely demonstrates that the modified peptide retains biological activity and exhibits therapeutic utility in various disease models. However, retention of activity following routine optimization for improved solubility and stability would have been reasonably expected in view of the teachings of Paraskevopoulos and Hong. To the extent Applicant demonstrates increased water solubility, such result is directedly taught and suggested by Paraskevopoulos, which expressly teaches that addition of terminal lysine residues increases aqueous solubility of peptides. Therefore, such evidence is consistent with, rather than contrary to, the expectations created by the prior art.
Further, although Applicant presents data relating to oral administration and comparisons to Ofev and Esbriet, the evidence does not establish that such results are unexpected relative to the closest prior art peptide lacking the claimed modifications. Evidence of therapeutic efficacy alone is insufficient where the prior art already suggested the claimed modifications for improving peptide pharmaceutical performance. Accordingly, the Declaration evidence is insufficient to rebut the strong prima facie case of obviousness established by the cited references.
Applicants’ arguments regarding the unpredictability of arriving at SEQ ID Nos:5-8 are also unpersuasive because the modifications applied to Beliveau’s peptide are limited and specifically guided by the teachings of the cited art. The claimed peptides represent predictable variations derived from applying known peptide engineering strategies to a known peptide scaffold. Accordingly, the rejection under 35 USC 103 maintained.
Conclusion
No claims are allowed.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERINNE R DABKOWSKI whose telephone number is (571)272-1829. The examiner can normally be reached Monday-Friday 7:30-5:30 Est.
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/ERINNE R DABKOWSKI/Examiner, Art Unit 1654
/LIANKO G GARYU/Supervisory Patent Examiner, Art Unit 1654
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