Prosecution Insights
Last updated: April 19, 2026
Application No. 17/768,166

TARGETED BIFUNCTIONAL DEGRADERS

Non-Final OA §103§112
Filed
Apr 11, 2022
Examiner
GOTFREDSON, GAREN
Art Unit
1619
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Yale University
OA Round
1 (Non-Final)
40%
Grant Probability
Moderate
1-2
OA Rounds
4y 0m
To Grant
70%
With Interview

Examiner Intelligence

Grants 40% of resolved cases
40%
Career Allow Rate
215 granted / 536 resolved
-19.9% vs TC avg
Strong +30% interview lift
Without
With
+29.5%
Interview Lift
resolved cases with interview
Typical timeline
4y 0m
Avg Prosecution
57 currently pending
Career history
593
Total Applications
across all art units

Statute-Specific Performance

§101
0.8%
-39.2% vs TC avg
§103
44.7%
+4.7% vs TC avg
§102
9.2%
-30.8% vs TC avg
§112
22.0%
-18.0% vs TC avg
Black line = Tech Center average estimate • Based on career data from 536 resolved cases

Office Action

§103 §112
DETAILED ACTION Claims 1, 4, 13, 16-31, 33-35, and 39 are pending. Of these, claims 33-35 and 39 are withdrawn as directed to a nonelected invention and claims 18 and 26-30 are withdrawn as directed to nonelected species. Therefore, claims 1, 4, 13, 16-17, 19-25, and 31 are under consideration on the merits. 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 . Election/Restriction Applicant’s election of Group I and the below species of compound of formula (I) is acknowledged: PNG media_image1.png 520 752 media_image1.png Greyscale The elections having been made without traverse, the restriction and election of species requirement are still considered proper and are made FINAL. Applicant asserts that claims 1, 4, 13, 16-27, and 31 read on the elected species. Examiner, however, does not understand claims 18 and 26-27 (drawn to CRBM binders that are not the elected binder to an asialoglycoprotein receptor) to read on the elected species of formula (I). Applicant is requested to ensure that the claim listing submitted with the response to this Office Action correctly identifies the claims that are withdrawn due to the species election. Information Disclosure Statement The information disclosure statement (IDS) submitted on 11/8/23, 10/2/23, 8/6/24, 12/23/24, 12/30/243/8/24, 5/8/25, and 10/9/15 was filed prior to the mailing date of a first Action on the merits. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, it was considered by the Examiner. Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. Claims 22 and 27 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 22 is indefinite because on page 18 of the claim listing it contains a table listing the identities of certain substituents, e.g., R1, R2, and R3, but the table is blurry such that much of it is illegible or barely legible, such that the metes and bounds of the claim are unclear. Additionally, the last portion of claim 22 on page 21, starting from the column labeled “R” with 16a through 16f, is also illegible or barely illegible. Therefore, the metes and bounds of claim 22 cannot be determined. Clarification is required. Claim 27 is similarly indefinite because on page 36 the figures and legends below the figures are illegible or barely legible. Therefore, the metes and bounds of claim 27 cannot be determined. Clarification is required. Examiner notes that the status of claim 27 as under examination is in dispute (see Restriction section, supra). To promote compact prosecution, claim 27 has been rejected under 25 USC 112(b) in case Applicant persuasively argues that claim 27 reads on the elected species of Formula (I). 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. Claims 1, 4, 13, 16-17, 19-25, and 31 are rejected under 35 U.S.C. 103 as unpatentable over Ribero (The Journal of Biological Chemistry Vol. 274, No. 19, (1999) pp. 13586-13593; of record in IDS dated 11/08/2022) in view of Khorev et al. (Bioorganic & Medicinal Chemistry 16 (2008) 6216-5231; of record in IDS dated 10/02/2023)) and Semple et al. (J Polym Sci Part A: Polymer Chemistry 2016 54, 2888-2895; of record in IDS dated 10/02/2023). As to claims 1, 4, 13, 16-17, 19-25, and 31, Rubeiro discloses that transforming growth factor-beta (TGF-B) is a peptide involved in the regulation of a variety of cellular functions including angiogenesis, embryogenesis, wound healing and inflammation (1st paragraph of body of the paper). Rubeiro states that modulating TGF-B activity in vivo would be beneficial in certain disorders such as fibrosis (last paragraph of paper on page 13593). Rubeiro teaches that one of the primary points of regulation of TGF-B is controlling its conversion from its latent precursor into its biologically active form, which is dependent on interaction of a specific amino acid sequence of thrombospondin-1 (i.e., KRFK) with a specific sequence in TGF-B (i.e., LSKL) which is flanked by the sequence RGQILSKLRL, which together form the elected species of protein binder, i.e., SEQ ID NO: 69 (Abstract; first full paragraph of left column of page 13587; first full paragraph of the right column of page 13589). Rubeiro further discloses dissolving the protein binder in PBS (a “pharmaceutically acceptable excipient”) so as to form a pharmaceutical composition of claim 31. As to claims 1, 4, 13, 16-17, 19-25, and 31, Rubeiro does not further expressly disclose that the elected species of protein binder (SEQ ID NO: 69) is bonded via the 1,2,3-triazole PEG adduct that is the elected species of linker to the triantennary N-acetyl galactosamine that is the elected species of cellular receptor binding moiety (CRBM) to form the elected species of formula (I) of claims 1, 4, 13, 6-17, and 19-25. Khorev discloses the synthesis of trivalent ligands comprised of beta-linked galactose or N-acetylated galactose (Gal/Gal/NAc) with a polyethylene glycol linker designed to bind with high affinity and specificity to the asialoglycoprotein receptor via the simultaneous interaction of 2-3 sugar residues with 2-3 binding sites on the receptor, and states that these ligands can be used as carriers for site-specific drug delivery to the liver (Abstract; paragraph bridging pages 5216-5217, Figure 1 and compound 4 of Figure 2). Khorev teaches that the asialoglycoprotein receptor is expressed on mammalian liver cells (“hepatocytes” of claim 16) and maintains serum glycoprotein homeostasis by recognizing, binding, and endocytosis of asialoglycoproteins, which, after internalization, are released into the acidic environment of an endosome and transported to lysosomes for degradation (first paragraph of Introduction section). Regarding the number of repeating residues in the PEG linker, the Office notes that homologs (compounds differing regularly by the successive addition of the same chemical group, e.g., by -CH2- groups) are generally of sufficiently close structural similarity that there is a presumed expectation that such compounds possess similar properties. In re Wilder, 563 F.2d 457, 195 USPQ 426 (CCPA 1977). See also In re May, 574 F.2d 1082, 197 USPQ 601 (CCPA 1978) (stereoisomers prima facie obvious). Semple discloses the synthesis of functionalized polyethylene glycol (PEG) azide derivatives, and teaches that such compounds are useful in the areas of bioconjugation chemistry and targeted drug delivery due to their ability to modify peptides and proteins (Abstract and Introduction Section). Semple further discloses synthesizing 1,2,3-triazole adducts from their corresponding PEG azides via a convenient click reaction (Abstract and Scheme 1). Semple teaches that the incorporation of such PEG derivatives into drug delivery systems improves pharmacological properties including increased water solubility, enhanced resistance to protein hydrolysis/degradation, improved bioavailability as measured by circulation half-life, and reduced antigenicity (Introduction Section). Regarding the number of repeating residues in the PEG portion of the derivative, the Office notes that homologs (compounds differing regularly by the successive addition of the same chemical group, e.g., by -CH2- groups) are generally of sufficiently close structural similarity that there is a presumed expectation that such compounds possess similar properties. In re Wilder, 563 F.2d 457, 195 USPQ 426 (CCPA 1977). See also In re May, 574 F.2d 1082, 197 USPQ 601 (CCPA 1978) (stereoisomers prima facie obvious). As to claims 1, 4, 13, 16-17, 19-25, and 31, it would have been prima facie obvious to one of ordinary skill in the art at the effective filing date of the present invention to modify the teachings of Rubeiro by connecting the peptide sequence taught by Rubeiro comprising SEQ ID: NO: 69 with the triantennary N-acetyl galactosamine that is the elected species of CRBM and via the 1,2,3-triazole PEG adduct that is the elected species of linker so as to arrive at the elected species of formula (I) of claims 1, 4, 13, and 16-30, because Rubeiro teaches that a peptide comprising SEQ ID: NO: 69 is capable of binding to thrombospondin-1, and Khorev teaches that trivalent ligands comprised of beta-linked galactose or N-acetylated galactose (Gal/Gal/NAc) can bind with high affinity and specificity to the asialoglycoprotein receptor via the simultaneous interaction of 2-3 sugar residues with 2-3 binding sites on the receptor, and Semple teaches that 1,2,3-triazole adducts formed from their corresponding PEG azides are useful in binding to peptides in bioconjugation chemistry to form delivery systems that have increased water solubility, enhanced resistance to protein hydrolysis/degradation, improved bioavailability as measured by circulation half-life, and reduced antigenicity. Therefore, the skilled artisan would have had a reasonable expectation of success in generating a compound with excellent pharmacological properties that is capable of binding to thrombospondin-1 and delivering it to the asialoglycoprotein receptor for degradation, by linking the Rubeiro amino acid sequence that binds to thrombospondin-1 to a triantennary N-acetyl galactosamine comprising the three sugar residues that Khorev teaches can bind with high affinity and specificity to the asialoglycoprotein receptor, and using as the linker the 1,2,3-triazole PEG adduct moiety that Semple teaches is useful in binding to peptides in bioconjugation chemistry and also advantageously forms delivery systems having improved pharmacological properties. The skilled artisan would have been motivated to formulate the foregoing delivery system in order to obtain the ability to modulate TGF-beta activity by delivering the protein responsible for its activation to the liver for degradation, in light of Ribeiro’s disclosure that modulating TGF-beta activity is useful in certain conditions such as in the presence of fibrosis. The skilled artisan alternatively would have been motivated to formulate the above delivery system to serve as a research tool to probe the activity of TGF-beta and/or thrombospondin-1. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to GAREN GOTFREDSON whose telephone number is (571)270-3468. The examiner can normally be reached on M-F 9AM-6PM. 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, David Blanchard can be reached on 5712720827. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see https://ppair-my.uspto.gov/pair/PrivatePair. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /GAREN GOTFREDSON/Examiner, Art Unit 1619 /ANNA R FALKOWITZ/ Primary Examiner, Art Unit 1600
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Prosecution Timeline

Apr 11, 2022
Application Filed
Jan 24, 2026
Non-Final Rejection — §103, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
40%
Grant Probability
70%
With Interview (+29.5%)
4y 0m
Median Time to Grant
Low
PTA Risk
Based on 536 resolved cases by this examiner. Grant probability derived from career allow rate.

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