一种TIMP2蛋白N端结构域的化学合成方法
By employing a segmented synthesis and natural chemical linking method, the efficient total synthesis of the N-terminal domain of the TIMP2 protein was successfully achieved, overcoming the limitation of synthetic length and preserving its biological activity. This lays the foundation for studying its interaction mechanism with MMP14 and developing inhibitors.
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- SOUTH CHINA UNIV OF TECH
- Filing Date
- 2026-02-25
- Publication Date
- 2026-07-17
AI Technical Summary
Existing technologies struggle to efficiently synthesize the N-terminal domain of long peptide chains, particularly in traditional solid-phase peptide synthesis methods limited to 50 amino acid lengths. Furthermore, the understanding of the interaction mechanism between TIMP2 and MMP14/MMP2 is incomplete, and there is a lack of ideas for developing specific inhibitors.
The N-terminal domain of the TIMP2 protein was synthesized in segments using the solid-phase peptide synthesis method SPPS and the natural chemical ligation reaction NCL. The amino acid sequence was divided into four fragments by the Fmoc solid-phase peptide synthesis method, and the correct disulfide bonds were formed by natural chemical ligation and refolding reaction, ensuring the efficiency and purity of the synthesis process.
This study achieved efficient total synthesis of the N-terminal domain of the TIMP2 protein, preserving its inhibitory activity against MMP14. It provides a tool for studying its mechanism of action and developing inhibitors, solves the problem of limited synthetic length, and improves yield and purity.
Smart Images
Figure CN122011162B_ABST