IP Library › Granted Patent US 12,622,951
Granted Patent B2
US 12,622,951 · App. 17/773,516 · Granted May 12, 2026

Urate oxidase-albumin conjugate, preparation method thereof, and use thereof

Inventors: Jeong Haeng Cho (Gimpo-si, KR); Sun Oh Shin (Gwangju, KR); Hyun Woo Kim (Seoul, KR); Hyeongseok Kim (Seoul, KR); Dong Ho Bak (Jeonju-si, KR); Inchan Kwon (Gwangju, KR); Byungseop Yang (Seoul, KR)
Assignee: ProAbtech Co., LTD.
A61K38/44A61K47/545A61K47/60A61K47/643A61P19/06C12N9/0048C12Y107/03003
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,622,951
App. No.
17/773,516
Granted
May 12, 2026
Kind
B2
Abstract

The present specification discloses a urate oxidase-albumin conjugate, a preparation method thereof, a urate oxidase variant contained in the urate oxidase-albumin conjugate, and a preparation method thereof. The urate oxidase-albumin conjugate is characterized in that three or more albumins are conjugated to the urate oxidase variant through a linker, thereby improving half-life and reducing immunogenicity. In addition, the urate oxidase-albumin conjugate can be used to prevent or treat various diseases, disorders and/or indications caused by uric acid.

Claims (34)

1 . A urate oxidase-albumin conjugate represented by [Formula 1]:

Uox-[J1-A-J2-HSA] n   [Formula 1]

wherein Uox is a urate oxidase variant, J1 is a urate oxidase-linker junction, A is an anchor, J2 is an albumin-linker junction, and HSA is Human Serum Albumin,

n is 3 or 4,

the urate oxidase variant is a tetramer formed by oligomerization of four urate oxidase variant subunits,

each of the urate oxidase variant subunit is a peptide independently selected from SEQ ID NOs:2 to 50, or a peptide which is 90% or more identical to the peptide selected from SEQ ID NOs:2 to 50,

the peptide selected from SEQ ID NOs:2 to 50 comprises a nonnatural amino acid X which is 4-(1,2,3,4-tetrazine-3-yl) phenylalanine (frTet),

the urate oxidase-linker junction is a structure formed through Inverse Electron Demand Diels-Alder (IEDDA) reaction between a tetrazine moiety of the nonnatural amino acid of the urate oxidase variant and a trans-cyclooctene moiety linked to the anchor,

the urate oxidase-linker junction is represented by following,

wherein the (1) is linked to the residue of the nonnatural amino acid, and the (2) is linked to the anchor,

wherein the anchor is selected from the following:

wherein J 1 is urate oxidase-linker junction, and J 2 is albumin-linker junction,

wherein the albumin-linker junction is a structure formed through a reaction between a thiol moiety of the albumin and a thiol reactive moiety of the anchor,

wherein the albumin-linker junction is selected from the following:

wherein (1) is linked to the albumin and (2) is linked to the anchor.

2 . The urate oxidase-albumin conjugate of claim 1 , wherein the urate oxidase variant comprises four urate oxidase variant subunit of SEQ ID NO: 49, wherein a nonnatural amino acid X of the SEQ ID NO: 49 is frTet.

3 . The urate oxidase-albumin conjugate of claim 1 , wherein the albumin is a sequence selected from SEQ ID NOs:133 to 144, or a sequence that is 90% or more identical to the sequence selected from SEQ ID NOs:133 to 144.

4 . A method for manufacturing a urate oxidase-albumin conjugate, the method comprising:

reacting an albumin and a linker, wherein the linker comprises a dienophile functional group, an anchor, and a thiol reactive moiety, wherein the dienophile functional group is a trans-cyclooctene or a derivative of trans-cyclooctene, and the thiol reactive moiety is selected from a maleimide or a derivative of maleimide, and a 3-arylpropiolonitriles or a derivative of 3-arylpropiolonitriles, wherein the thiol reactive moiety of the linker is bound with thiol moiety of albumin through reaction to form an albumin-linker conjugate; and

reacting the albumin-linker conjugate and the urate oxidase variant, wherein the urate oxidase is a tetramer in which four urate oxidase subunits are oligomerized,

wherein each of the urate oxidase subunit is represented by a sequence independently selected from SEQ ID NOs:2 to 50, or a sequence that is 90% or more identical to the sequence selected from SEQ ID NOs:2 to 50,

wherein the X of a sequence of SEQ ID NOs:2 to 50 is nonnatural amino acid which is 4-(1,2,3,4-tetrazine-3-yl) phenylalanine (frTet),

wherein the urate oxidase variant comprises four frTets,

wherein a tetrazine functional group of a residue of the frTet is bound with the dienophile functional group of the linker through Inverse Electron Demand Diels-Alder (IEDDA) reaction to form a urate oxidase-albumin conjugate, and

wherein the urate oxidase-albumin conjugate is characterized in that three or more albumins are conjugated to the urate oxidase variant through the linkers.

5 . The method of claim 4 , the linker is selected from the following:

6 . The method of claim 4 , wherein the urate oxidase variant is a tetramer that four urate oxidase variant subunits represented by SEQ ID NO: 29 are oligomerized, wherein the X of SEQ ID NO: 29 is frTet.

7 . The method of claim 4 , wherein the albumin is represented by a sequence selected from SEQ ID NOs: 133 to 144 or a sequence 90% or more identical with the sequence selected from SEQ ID NOs: 133 to 144, wherein the thiol reactive moiety of the linker is bound with thiol group of 34th cysteine of the sequence of the albumin through reaction.

8 . The method of claim 4 , wherein the reacting of the urate oxidase variant with the linker is performed at pH of 6 to 8.

9 . A method for treating uric acid-related disease, the method comprising:

administering the urate oxidase-albumin conjugate of claim 1 into a subject.

10 . The method of claim 9 , wherein the uric acid-related disease is any one of hyperuricemia, acute gouty arthritis, intermittent gout, chronic nodular gout, Chronic Kidney Disease, and Tumor Lysis Syndrome (TLS).

11 . The method of claim 9 , wherein the administering the pharmaceutical composition into a subject is selected from oral administration, parenteral administration, intravenous administration, intravenous infusion, intraperitoneal administration, intramuscular administration, transdermal administration, and subcutaneous administration.

12 . The method of claim 9 , wherein the dosage of the pharmaceutical composition is 1 mg/kg to 10 mg/kg, based on the mass of the administered urate oxidase-albumin conjugate relative to the mass of the subject.

Assignments (3)
CHANGE OF NAME Recorded Jan 15, 2025
From: PROABTECH INC.
To: PROABTECH CO., LTD.
Reel/Frame 069930/0818 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jun 14, 2023
From: YANG, BYUNGSEOP
To: PROABTECH INC.
Reel/Frame 063945/0517 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 20, 2022
From: CHO, JEONG HAENG; SHIN, SUN OH; KIM, HYUN WOO; KIM, HYEONGSEOK; BAK, DONG HO; KWON, INCHAN
To: PROABTECH INC.
Reel/Frame 060764/0239 →
Priority Claims (2)
KR 10-2020-0125215 · Sep 25, 2020 · national
KR 10-2021-0013537 · Jan 29, 2021 · national
Continuity (1)
Related Publication 20230211002A1 · Jul 6, 2023
References Cited (44)
US 8962811B2 · Kieliszewski et al. · 2015 [cited by applicant]
US 12161699B2 · Cho et al. · 2024 [cited by applicant]
US 20130209466A1 · Walker et al. · 2013 [cited by applicant]
US 20140066378A1 · Dixit et al. · 2014 [cited by applicant]
US 20170175183A1 · Ju et al. · 2017 [cited by applicant]
US 20190077776A1 · Mehl et al. · 2019 [cited by applicant]
US 20200010450A1 · Yang et al. · 2020 [cited by applicant]
US 20230149517A1 · Cho et al. · 2023 [cited by applicant]
US 20230211002A1 · Cho et al. · 2023 [cited by applicant]
CN 102627615A · 2012 [cited by applicant]
EP 4218825A1 · 2023 [cited by applicant]
EP 4282876A1 · 2023 [cited by applicant]
KR 1020110128827A · 2011 [cited by applicant]
KR 1020150124999A · 2015 [cited by applicant]
KR 101637010B1 · 2016 [cited by applicant]
KR 1020180002828A · 2018 [cited by applicant]
KR 1020190045116A · 2019 [cited by applicant]
WO WO2015054658A1 · 2015 [cited by applicant]
WO WO2021246557A1 · 2021 [cited by applicant]
WO WO2022065913A1 · 2022 [cited by applicant]
Gil et al., “Bioengineered robust hybrid hydrogels enrich the stability and efficacy of biological drugs”, Journal of Controlled Release 267: 119-132 (Year: 2017). [cited by examiner]
Bak et al., “Recombinant peptide production platform coupled with site-specific albumin conjugation enables a convenient production of long-acting therapeutic peptide”, Pharmaceutics 12(4): 364 (2020). [cited by applicant]
International Search Report and Written Opinion for International Application No. PCT/KR2021/013077 dated Jan. 24, 2023. [cited by applicant]
International Search Report and Written Opinion for International Application No. PCT/KR2022/001675 dated Dec. 27, 2022. [cited by applicant]
International Search Report and Written Opinion for International Application No. PCT/KR2022/009593 dated Oct. 14, 2022. [cited by applicant]
International Search Report and Written Opinion for International Application No. PCT/KR2022/014276 dated Dec. 27, 2022. [cited by applicant]
Kolodych et al. “CBTF: new amine-to-thiol coupling reagent for preparation of antibody conjugates with increased plasma stability.” Bioconjugate chemistry 26.2 (2015): 197-200. [cited by applicant]
NCBI, Genbank accession No. 1AO6_A. [cited by applicant]
NCBI, Genbank accession No. E13225. [cited by applicant]
Yang et al., “Multivalent Albumin-Neonatal Fc Receptor Interactions Mediate a Prominent Extension of the Serum Half-Life of a Therapeutic Protein”, Molecular Pharmaceutics 18.6 : 2397-2405 (2021). [cited by applicant]
Yang et al., “Temporal control of efficient in vivo bioconjugation using a genetically encoded tetrazine-mediated inverse-electron-demand Diels-Alder reaction.” Bioconjugate Chemistry 31.10 (2020): 2456-2464. [cited by applicant]
Lim et al., “Site-specific albumination of a therapeutic protein with multi-subunit to prolong activity in vivo,” Journal of Controlled Release 207 (2015): 93-100. [cited by applicant]
Shi et al., “Structure-based design of a hyperthermostable AgUricase for hypemricemia and gout therapy”, Acta Pharmacologica Sinica., 40(10): 1364-1372 (2019). [cited by applicant]
International Search Report and Written Opinion for PCT/KR2021/013037 with translated Search Report dated Jan. 24, 2022. [cited by applicant]
Cho, Jeong-Haeng et al. “Optimization of Cultivation Conditions for Production of Recombinant Urate Oxidase with Unnatural Amino Acids”, KSBB Journal 35.1: 51-56 (2020). [cited by applicant]
Cho et al., “Albumin affibody-outfitted injectable gel enabling extended release of urate oxidase-albumin conjugates for hyperuricemia treatment,” Journal of Controlled Release 324 (2020): 532-544. [cited by applicant]
Poznansky et al., “Biological macromolecules as carriers of drugs and enzymes,” Drug Delivery Systems: Characteristics and Biomedical Applications (1980): 253-315. [cited by applicant]
Remy et al., “Immunogenicity and Antigenicity of Soluble Cross-Linked Enzyme/AlbuminPolymers” Advantages for Enzyme Therapy, The Lancet 312.8080 (1978): 68-70. [cited by applicant]
Supplementary European Search Report for EP Application No. 21872941.6 dated May 14, 2025. [cited by applicant]
Supplementary European Search Report for EP Application No. 21872964.8 dated Feb. 17, 2025. [cited by applicant]
Blizzard et al., “Ideal bioorthogonal reactions using a site-specifically encoded tetrazine amino acid”, Journal of the American Chemical Society 137.32: 10044-10047(2015). [cited by applicant]
Blizzard, “In Vivo Reactions of Tetrazines Incorporated through Genetic Code Expansion”, Oregon State University Biochemistry and Biophysics Doctor of Philosophy (Ph.D.) Dissertation, pp. 1-133 (2019). [cited by applicant]
Office Action for Korean Application No. 10 2023/7009860 dated Mar. 22, 2023. [cited by applicant]
Rajbhandary, “Site Specific Incorporation of Amino Acid Analogues into; Proteins In Vivo” Final Report, 137(32), pp. 1-55, (2010). [cited by applicant]