Prosecution Insights
Last updated: October 25, 2026
Application No. 18/448,427

Peptide Sequences And Compositions At Air-Aqueous Interfaces For Lanthanide Recovery

Final Rejection §102§103§112
Filed
Aug 11, 2023
Priority
Aug 11, 2022 — provisional 63/371,080 +1 more
Examiner
KONOPELSKI SNAVEL, SARA ELIZABETH
Art Unit
1658
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Northwestern University
OA Round
2 (Final)
35%
Grant Probability
At Risk
3-4
OA Rounds
6m
Est. Remaining
70%
With Interview

Examiner Intelligence

Grants only 35% of cases
35%
Career Allowance Rate
14 granted / 40 resolved
-25.0% vs TC avg
Strong +35% interview lift
Without
With
+35.4%
Interview Lift
resolved cases with interview
Typical timeline
3y 9m
Avg Prosecution
51 currently pending
Career history
102
Total Applications
across all art units

Statute-Specific Performance

§101
7.4%
-32.6% vs TC avg
§103
27.6%
-12.4% vs TC avg
§102
18.2%
-21.8% vs TC avg
§112
26.1%
-13.9% vs TC avg
Black line = Tech Center average estimate • Based on career data from 40 resolved cases

Office Action

§102 §103 §112
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 . Objections/Rejections Withdrawn Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application. Response to Arguments Applicant's arguments filed 8/3/2026, with respect to the claim rejections under 35 U.S.C. 102 and 103, have been fully considered but they are not persuasive. Applicant’s position is that none of the references currently on the record disclose a peptide-comprising surfactant. However, there is nothing in the present application to suggest that the claimed-peptide comprising surfactants are anything more than peptide surfactants described in the prior art, wherein a portion of the amino acid sequence of the peptide constitutes or acts as the surfactant. The instant specification only provides support for this type of peptide-comprising surfactant; the instant Examples indicate SEQ ID NO: 1-3 are capable of adsorption to Tb3+ cations at air-aqueous interfaces ([00145-00178]; also see, for instance, Figures 2, 6, 14, and 19). Although cosurfactants are briefly mentioned in [0013], they are not expressly claimed, and the instant specification does not provide any structural information about them. Effectively, what is discussed in the Remarks is not commensurate in scope with the claims nor what is disclosed in the instant specification. For this reason, the rejections have been maintained/modified below. Claim Status Claims 1-20 are pending. 1, 3, 7, 11, and 17 are currently amended. Priority The instant application claims priority to the provisional applications 63/400,695, filed 8/24/2022, and 63/371,080, filed 8/11/2022. The priority date of 8/11/2022 is acknowledged. Claim Interpretation Claims 1-20 are drawn to a method of complexing a peptide surfactant (PEPS; also referred to as a peptide-comprising surfactant) to a rare earth element (REE), wherein the PEPS comprises a REE-binding region that preferentially binds to one or more REEs, as well as a composition comprising a PEPS and a REE, wherein the PEPS comprises at least one lanthanide binding tag (LBT) comprising one or more residues arranged in a binding region that coordinates with an REE cation to form a PEPS-REE complex. The instant specification teaches that PEPS include a hydrophilic amino acid sequence that selectively binds an REE cation and a hydrophobic sequence that confers surface activity ([0008]). REEs are elements between Lanthanum and Lutetium on the periodic table, also known as Lanthanides. Yttrium and Scandium are often included in this category of elements as they share chemical and physical properties with the group that exist in nature with other Lanthanides (Ln3+) ([0091]). Thus, the PEPS, as recited in the claims, is being interpreted as comprising a hydrophilic amino acid sequence capable of binding to Lathanides, Yttrium, or Scandium (Lanthanides only, where specified) and a hydrophobic moiety. Claim 6 recites the method of claim 1 further comprising effecting disposition of the PEPS-REE complex to an air/liquid interface. This claim is being interpreted as the complexing of PEPS to a REE in solution results in the incorporation of the complex into an air/liquid interface. 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 1-20 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. Claims 1 and 11 both recite the PEPS comprises a peptide having the sequence of one of SEQ ID NO: 1-46. Per the Sequence Listing, the amino acid sequences of both SEQ ID NO: 4 and SEQ ID NO: 5 each include one X residue and a notation indicating that tryptophan binds to acridonylalanine. These limitations render the scope of these claims indefinite because X is undefined and it is unclear how tryptophan binds to acriodonylalanine as neither amino acid is recited in either sequence. For purposes of examination, the X residue in SEQ ID NO: 4 and 5 will be interpreted as open to any amino acid. Further, by virtue of their dependency on claims 1 and 11, claims 2-10 and 12-20 are also hereby rejected for this same reasoning. Claim Rejections - 35 USC § 102 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. (a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention. SEQ ID NO: 1 and 4 Claim(s) 1-5, 11, and 16 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Boyle et al. (US20220348619A1, effectively filed 6/21/2019). Boyle teaches rare earth element (REE)-binding proteins (e.g., lanthanide-binding proteins; “PEPS”), host cells expressing REE-binding proteins, and methods of recovering REEs (Abstract). Regarding claim 1, Boyle teaches methods of recovery of REEs from a sample such as a mine or a waste stream (solution; [0118]); samples can also come from a stream, pond, river, creek or other waterways ([0087]). The method comprises applying REE-binding proteins or cells containing REE-binding proteins to said sample wherever the sample is located ([0118-0119]). Boyle further teaches that the REE-binding proteins may be capable of binding one or more REEs ([0043]). Boyle teaches SEQ ID NO: 2, which comprises the instant SEQ ID NO: 1 as well as the instant SEQ ID NO: 4 wherein X is a Trp residue. Regarding claim 2, Boyle teaches the REE-binding region can comprise a lanthanide binding tag (LBT; [0014]). Regarding claim 3, Boyle teaches many LBTs that further comprise at least one additional hydrophobic moiety. For instance, SEQ ID NO: 2 of Boyle encompasses the instant SEQ ID NO: 1/SEQ ID NO: 4(highlighted segment of the sequence): PNG media_image1.png 462 550 media_image1.png Greyscale and the hydrophobic moiety “GPG” is immediately N-terminal to the instant SEQ ID NO: 1; additionally, “M” is C-terminal to SEQ ID NO: 1/4. Regarding claim 4, in another example taught by Boyle, SEQ ID NO: 1/4 comprises the following sequence: PNG media_image2.png 448 558 media_image2.png Greyscale , where the shorter sequence is the hydrophobic moiety (Ala Ala Phe), the longer highlighted sequence is the REE-binding motif (Asp Pro… Glu Leu), and the intervening sequence is the spacer (Asp Lys Leu). Regarding claim 5, Boyle teaches in some embodiments the REE binding protein is a lanthanide binding protein. In some embodiments, the REE binding protein is a yttrium binding protein. In some embodiments, the REE binding protein is a scandium binding protein ([0014]). This reads on REE binding proteins having preference for one type of REE over another. Regarding claim 11, Boyle teaches performing a binding assay between identified REE-binding proteins and terbium and/or dysprosium, both REEs (Example 1 [0128-0130]; Figures 3 and 4; Example 2 [0132-0135]; Figures 5 and 6). Additionally, as stated above, Boyle teaches SEQ ID NO: 2, which comprises the instant SEQ ID NO: 1/SEQ ID NO: 4 wherein X is a Trp residue. Regarding claim 16, as stated above, Boyle teaches in some embodiments the REE binding protein is a lanthanide binding protein. In some embodiments, the REE binding protein is a yttrium binding protein. In some embodiments, the REE binding protein is a scandium binding protein ([0014]). This reads on REE binding proteins having preference for one type of REE over another. Claim Rejections - 35 USC § 103 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. SEQ ID NO: 2, 3, 5-13, 16-22, 25-35 and 38 Claim(s) 1-5, 11, and 16 are rejected under 35 U.S.C. 103 as being unpatentable over Boyle et al. (US20220348619A1, effectively filed 6/21/2019). The teachings of Boyle have been set forth above. Boyle does not expressly teach SEQ ID NO: 2, 3, 5-13, 16-22, 25-35 and 38. The differences between these instant SEQ ID NO’s and SEQ ID NO: 2 of Boyle are shown below: SEQ ID NO: 2 PNG media_image3.png 212 772 media_image3.png Greyscale ; SEQ ID NO: 3 PNG media_image4.png 206 782 media_image4.png Greyscale ; SEQ ID NO: 5 PNG media_image5.png 216 802 media_image5.png Greyscale , wherein X is any amino acid; SEQ ID NO: 6 PNG media_image6.png 218 782 media_image6.png Greyscale ; SEQ ID NO: 7 PNG media_image7.png 202 798 media_image7.png Greyscale ; SEQ ID NO: 8 PNG media_image8.png 208 782 media_image8.png Greyscale ; SEQ ID NO: 9 PNG media_image9.png 208 788 media_image9.png Greyscale ; SEQ ID NO: 10 PNG media_image10.png 214 778 media_image10.png Greyscale ; SEQ ID NO: 11 PNG media_image11.png 214 786 media_image11.png Greyscale ; SEQ ID NO: 12 PNG media_image12.png 202 790 media_image12.png Greyscale ; SEQ ID NO: 13 PNG media_image13.png 206 778 media_image13.png Greyscale ; SEQ ID NO: 16 PNG media_image14.png 222 790 media_image14.png Greyscale ; SEQ ID NO: 17 PNG media_image15.png 202 806 media_image15.png Greyscale ; SEQ ID NO: 18 PNG media_image16.png 210 776 media_image16.png Greyscale ; SEQ ID NO: 19 PNG media_image17.png 200 776 media_image17.png Greyscale ; SEQ ID NO: 20 PNG media_image18.png 200 788 media_image18.png Greyscale ; SEQ ID NO: 21 PNG media_image19.png 226 794 media_image19.png Greyscale ; SEQ ID NO: 22 PNG media_image20.png 202 782 media_image20.png Greyscale ; SEQ ID NO: 25 PNG media_image21.png 200 778 media_image21.png Greyscale ; SEQ ID NO: 26 PNG media_image22.png 188 802 media_image22.png Greyscale ; SEQ ID NO: 27 PNG media_image23.png 200 776 media_image23.png Greyscale ; SEQ ID NO: 28 PNG media_image24.png 244 790 media_image24.png Greyscale ; SEQ ID NO: 29 PNG media_image25.png 194 790 media_image25.png Greyscale ; SEQ ID NO: 30 PNG media_image26.png 206 770 media_image26.png Greyscale ; SEQ ID NO: 31 PNG media_image27.png 210 812 media_image27.png Greyscale ; SEQ ID NO: 32 PNG media_image28.png 208 786 media_image28.png Greyscale ; SEQ ID NO: 33 PNG media_image29.png 206 792 media_image29.png Greyscale ; SEQ ID NO: 34 PNG media_image30.png 190 788 media_image30.png Greyscale ; SEQ ID NO: 35 PNG media_image31.png 208 792 media_image31.png Greyscale ; and SEQ ID NO: 38 PNG media_image32.png 208 790 media_image32.png Greyscale . Boyle further teaches that the skilled artisan will also realize that mutations in a recombinant peptide or polypeptide coding sequence may result in conservative amino acid substitutions to provide functionally equivalent variants of such a peptide or polypeptide, i.e., variants that retain the same or similar activity. A “conservative amino acid substitution” refers to an amino acid substitution that does not alter the relative charge or size characteristics or functional activity of the protein in which the amino acid substitution is made. Boyle further describes that 1-20 or more residues can be changed, i.e., replaced by conservative amino acid substitutions that can be prepared according to methods known to one of ordinary skill in the art ([0078-0082]; Table 1). Consequently, it would be prima facie obvious to substitute the residue(s) that are different from SEQ ID NO: 2 of Boyle, shown above, for a conservative residue(s), thereby resulting in the instant SEQ ID NO: 2, 3, 5-13, 16-22, 25-35 and 38. One skilled in the art would be motivated to do so and have a reasonable expectation of success because Boyle taught that such conservative substitutions could be readily made in PEPS that would conserve the function of said PEPS while producing a different structural variant. It would also be obvious to substitute the residues different from SEQ ID NO: 2 of Boyle for conservative substitutions because one skilled in the art would readily know and recognize the differences between the instantly claimed peptides and SEQ ID NO: 2 of Boyle as conservative substitutions; one would also know that conservative substitutions are useful to generate structural variants of peptides while retaining their functionality. Boyle also indicates that for each amino acid, there are only a few options that constitute a conservative amino acid substitution, thereby making the possibilities finite. Because of this, one skilled in the art would have a reasonable expectation of introducing a conservative substitution into SEQ ID NO: 6, 10, 13, and/or 16 and retaining its functionality as a PEPS, thereby making it obvious to try. See MPEP 2143(I)(E). Regarding claim 2, Boyle teaches the REE-binding region can comprise a lanthanide binding tag (LBT; [0014]). Regarding claim 3, Boyle teaches many LBTs that further comprise at least one additional hydrophobic moiety. For instance, in SEQ ID NO: 2 of Boyle, shown below: PNG media_image1.png 462 550 media_image1.png Greyscale the hydrophobic moiety “GPG” is immediately N-terminal to the instant SEQ ID NO: 2, 3, 5-13, 16-22, 25-35 and 38. Regarding claim 4, another example taught by Boyle is the following sequence: PNG media_image2.png 448 558 media_image2.png Greyscale , where the shorter sequence is the hydrophobic moiety (Ala Ala Phe), the longer highlighted sequence is the REE-binding motif (Asp Pro… Glu Leu), and the intervening sequence is the spacer (Asp Lys Leu). Regarding claim 5, Boyle teaches in some embodiments the REE binding protein is a lanthanide binding protein. In some embodiments, the REE binding protein is a yttrium binding protein. In some embodiments, the REE binding protein is a scandium binding protein ([0014]). This reads on REE binding proteins having preference for one type of REE over another. Regarding claim 11, Boyle teaches performing a binding assay between identified REE-binding proteins and terbium and/or dysprosium, both REEs (Example 1 [0128-0130]; Figures 3 and 4; Example 2 [0132-0135]; Figures 5 and 6). Additionally, as stated above, Boyle renders the instant SEQ ID NO: 2, 3, 5-13, 16-22, 25-35 and 38 obvious. Regarding claim 16, as stated above, Boyle teaches in some embodiments the REE binding protein is a lanthanide binding protein. In some embodiments, the REE binding protein is a yttrium binding protein. In some embodiments, the REE binding protein is a scandium binding protein ([0014]). This reads on REE binding proteins having preference for one type of REE over another. SEQ ID NO: 1-13, 16-22, 25-35 and 38 Claim(s) 1-20 are rejected under 35 U.S.C. 103 as being unpatentable over Boyle et al. (US20220348619A1, effectively filed 6/21/2019) in view of Shetty et al. (Foam flotation of rare earth elements by conventional and green surfactants, 2020, Minerals Engineering, vol. 158, p. 1-9; cited on IDS filed 1/29/2024 as “Sharath et al.”). The teachings of Boyle have been set forth above. Boyle does not teach a method wherein a PEPS is complexed to a REE effecting disposition of the PEPS-REE complex to an air/liquid interface. Shetty teaches foam (ion and precipitate) flotation is a promising green method of recovery for REEs from leachates of the primary and secondary resources (Abstract). In ion flotation, target ions adsorb on the headgroups of surfactant films that stabilize bubbles dispersed in solution (air-water interface). In precipitate flotation, target ions attach to these bubbles with or without surfactants. The loaded bubbles rise to the top of the cell where they are collected as a foam. Both ion and precipitate flotation employ surfactants as collectors and rely on bubbles and gravity, but instead of dispersed mineral particles, they separate dissolved ions from their mixture. As it can be difficult to differentiate a priori ion and precipitate flotation from each other in practice, collectively they are referred to as “foam” flotation (Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Foam flotation has several advantages over solvent extraction such as lower water consumption, facile and flexible operation, lower energy consumption, lower sludge, lower operational costs, and no toxic or hazardous chemicals and solvents. It can also be applied to a wide range of ion concentrations and the used surfactants and water can be recovered and recycled (Pg 2, left column, second paragraph). In summary, Boyle teaches a method of complexing PEPS with REEs. Shetty teaches foam flotation, which is a method designed to recover REEs from solution by introducing surfactants that bind to said REEs and bubbles that the surfactants, by extension the REEs, can attach to generate a collectable foam. Thus, regarding claim 6, it would be prima facie obvious to incorporate the foam flotation method taught by Shetty, which effects disposition of the PEPS-REE complex to an air/liquid interface, into the PEPS-REE complexing method taught by Boyle. One would be motivated to do so in order to take advantage of the benefits of foam filtration, as listed above and taught by Shetty. One would have a reasonable expectation of success as Shetty teaches surfactants and their properties (ability to bind REEs and bubbles) are key to practicing this method, and Boyle teaches surfactants, namely, PEPS. Additionally, it would be prima facie obvious to substitute the surfactant taught by Shetty for the PEPS taught by Boyle. One skilled in the art would recognize that both types of surfactants served the same purpose: to complex REEs and adsorb to bubbles for the removal and recovery of REEs from solution. Therefore, it would be obvious to substitute one type of surfactant for another. See MPEP 2143(I)(B). Moreover, it would be obvious to try to substitute the surfactants taught by Shetty for a PEPS taught by Boyle. Shetty teaches that in the foam flotation of REEs, only a few surfactants have been tested so far but green alternatives are still needed (Pg 2, left column, final paragraph – right column, first paragraph). Given that PEPS are composed of naturally-occurring, proteinogenic amino acids and exhibit surfactant properties, it would be obvious to try a PEPS in the foam filtration method taught by Shetty. See MPEP 2143(I)(E). Regarding claim 7, as stated above, Shetty teaches the air/liquid interface is present at bubbles (Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claims 8 and 9, as stated above, Shetty teaches foam flotation, specifically ion flotation, results in the production of a surfactant film, which comprises a plurality of PEPS-REE complexes (aggregates; Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claim 10, as stated above, Shetty teaches sparging bubbles through solution such that the PEPS-REE complex adsorbs to bubbles, creating a foam that can be collected (recovering the REE cation; Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claims 12 and 13, as stated above, Shetty teaches a method of foam flotation, which creates a composition comprising a complex comprising PEPS and REE, wherein the composition comprises a film which comprises a plurality of PEPS-REE complexes (aggregates; Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claim 14, as stated above, Shetty teaches PEPS-REE complexes are disposed at an air/liquid interface (Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claim 15, Shetty further teaches PEPS-REE complexes can be disposed at air/water interfaces (Pg 2, 5th paragraph). Regarding claim 17, as stated above, Shetty teaches PEPS-REE complexes that occur at an air/liquid interface that defines a bubble (Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claims 18 and 19, Shetty teaches the PEPS-REE complexes are initially disposed within solution and then form a foam (Pg 1, Introduction, right column, second paragraph – Pg 2, left column, first paragraph). Regarding claim 20, although not expressly taught by Boyle or Shetty, it would be obvious that the composition comprising complexed PEPS-REE would be net-neutral or net-positive. One skilled in the art would recognize that REEs are positively charged and complexation of PEPS and REE is mediated by their charge differences; thus, one would expect a composition comprising PEPS-REEs to be neutral to positive. Allowable Subject Matter Peptides comprising SEQ ID NO: 14, 15, 23, 24, 36, 37, and 39-46 and methods of use thereof are free of the art. Regarding SEQ ID NO: 14, 15, 23, 24, 36, 37, the closest art for each is SEQ ID NO: 2 of Boyle, described above, with 88.8-95.9% sequence identity. The differences between SEQ ID NO: 2 of Boyle and each of the instant SEQ ID NO: 14, 15, 23, 24, 36, and 37 are shown below: SEQ ID NO: 14 PNG media_image33.png 158 578 media_image33.png Greyscale SEQ ID NO: 15 PNG media_image34.png 146 572 media_image34.png Greyscale SEQ ID NO: 23 PNG media_image35.png 146 566 media_image35.png Greyscale SEQ ID NO: 24 PNG media_image36.png 150 572 media_image36.png Greyscale SEQ ID NO: 36 PNG media_image37.png 152 548 media_image37.png Greyscale ; and SEQ ID NO: 37 PNG media_image38.png 153 566 media_image38.png Greyscale . Regarding SEQ ID NO: 42-45, the closest art for each is SEQ ID NO: 1 of Boyle, described above, with 66.3-71.9% sequence identity. The differences between SEQ ID NO: 1 of Boyle and each of the instant SEQ ID NO: 42-45 are shown below: SEQ ID NO: 42 PNG media_image39.png 136 548 media_image39.png Greyscale ; SEQ ID NO: 43 PNG media_image40.png 144 544 media_image40.png Greyscale ; SEQ ID NO: 44 PNG media_image41.png 134 582 media_image41.png Greyscale ; and SEQ ID NO: 45 PNG media_image42.png 142 542 media_image42.png Greyscale . Regarding SEQ ID NO: 39-41 and 46, the closest art for each is SEQ ID NO: 5 of Jiao et al. (US20180195147A1, published 7/12/2018), with 72.2-81.4% sequence identity. The differences between SEQ ID NO: 5 of Jiao and each of the instant SEQ ID NO: 39-41 and 46 are shown below: SEQ ID NO: 39 PNG media_image43.png 160 628 media_image43.png Greyscale ; SEQ ID NO: 40 PNG media_image44.png 142 544 media_image44.png Greyscale ; SEQ ID NO: 41 PNG media_image45.png 152 558 media_image45.png Greyscale ; and SEQ ID NO: 46 PNG media_image46.png 148 550 media_image46.png Greyscale . For each of the above peptides, at least one internal, non-conservative substitution has been made; several peptides have an internal, non-conservative substitution in addition to removal of 1-2 amino acids from both the N- and C- termini. Based on the teachings of Boyle and other PEPS art, it is not obvious to make such substitutions and deletions; therefore, SEQ ID NO: 14, 15, 23, 24, 36, 27 and 39-46 and methods of use thereof are novel and non-obvious. Conclusion No claim is allowed. Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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 Sara Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa L Fisher can be reached at 571-270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658 /Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
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Prosecution Timeline

Aug 11, 2023
Application Filed
Jun 08, 2026
Non-Final Rejection mailed — §102, §103, §112
Aug 03, 2026
Response Filed
Oct 16, 2026
Final Rejection mailed — §102, §103, §112 (current)

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Prosecution Projections

3-4
Expected OA Rounds
35%
Grant Probability
70%
With Interview (+35.4%)
3y 9m (~6m remaining)
Median Time to Grant
Moderate
PTA Risk
Based on 40 resolved cases by this examiner. Grant probability derived from career allowance rate.

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