Anti-coagulant protein triabin containing tyrosine sulfation modification and semi-chemical synthesis method thereof

CN122103315AActive Publication Date: 2026-05-29SOUTH CHINA UNIV OF TECH
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
SOUTH CHINA UNIV OF TECH
Filing Date
2026-04-28
Publication Date
2026-05-29

AI Technical Summary

Technical Problem

Existing technologies make it difficult to efficiently prepare Triabin protein with uniform tyrosine sulfate modification through chemical synthesis, which limits its development in anticoagulant activity research and clinical application.

Method used

Triabin was synthesized by using Fmoc peptide solid-phase synthesis and E. coli recombinant expression technology to divide it into two fragments. Fragment 1 and fragment 2 were synthesized and purified respectively. The tyrosine-sulfated modified Triabin was synthesized through natural chemical linkage and refolding reaction.

Benefits of technology

This study improved the synthesis efficiency and stability of tyrosine-sulfated Triabin protein, enhanced its anticoagulant activity, provided a homogenized preparation method, and laid the foundation for the development of clinical anticoagulant drugs.

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Abstract

The application provides an anti-coagulation protein Triabin containing a tyrosine sulfation modification and a semi-chemical synthesis method thereof. According to the distance, the Triabin is divided into fragment 1 and fragment 2 according to the closest cysteine to a sulfated tyrosine site, the sulfated tyrosine site is located in the fragment 1, and the sulfated tyrosine site is close to the C-terminal of the fragment 1; the polypeptide solid-phase synthesis technology is used to synthesize a fragment 1 polypeptide resin, and after cleavage, deprotection, extraction and purification, the fragment 1 with an amide C-terminal is obtained; the E. coli recombinant expression technology is used to obtain the fragment 2 with a hydrazine C-terminal; the thioester of the fragment 2 with the hydrazine C-terminal is converted, the natural chemical linking reaction and the neopentyl removal reaction are used to obtain a full-length linear protein, and the anti-coagulation protein Triabin containing the tyrosine sulfation modification is obtained through a refolding reaction. The anti-coagulation protein Triabin containing the tyrosine sulfation modification has stronger anti-coagulation activity than the wild-type Triabin.
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Citation Information

Patent Citations

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