anxa1 derived polypeptide and its application

A peptide and peptide sequence technology, applied in the field of anti-tumor ANXA1-derived peptides, can solve the problems of specificity and safety defects, and the biological significance of protein interaction has not been reported.

Active Publication Date: 2021-01-29
XIANGYA HOSPITAL CENT SOUTH UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Although EphA2 inhibitors such as ALW-II-41-27 have entered clinical trials, their specificity and safety still have major defects
[0004] Both ANXA1 and EphA2 are potential tumor intervention targets, but the interaction between these two proteins and their biological significance have not been reported so far

Method used

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  • anxa1 derived polypeptide and its application
  • anxa1 derived polypeptide and its application
  • anxa1 derived polypeptide and its application

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Embodiment 1

[0134]Example 1: Anti-Nasopharyngeal Carcinoma Effect of N-terminal 20-30 Amino Acid Polypeptides of ANXA1

[0135]The target peptide sequence used in the embodiment of the present invention is the sequence of the amino acid sequence at positions 20-30 of the N-terminal of ANXA1 and the commonly used transmembrane peptide TAT:

[0136]Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Glu-Tyr-Val-Gln-Thr-Val-Lys-Ser-Ser-Lys-Gly, the single letter sequence is YGRKKRRQRRR- EYVQTVKSSKG, with a purity of more than 95% and good water solubility, is synthesized by Suzhou Qiangyao Biological Company.

[0137]Figure 8A is the peptide design diagram. The N-terminal 20-30 amino acid sequence [A1(20-30)] of TAT connected to ANXA1 is the target peptide, the sequence is YGRKKRRQRRREYVQTVKSSKG, and the purity is above 96%. The control peptide TAT sequence is YGRKKRRQRRR, with a purity of over 96%. The designed peptide was synthesized by Suzhou Qiangyao Biological Company.

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Abstract

The invention provides an anti-tumor ANXA1 derived polypeptide and its application. A series of experimental results confirmed that ANXA1 protects EphA2 from being ubiquitinated and degraded by E3 ubiquitin ligase Cbl by binding to EphA2. ) is the key region for the combination of ANXA1 and EphA2. In order to block the combination of ANXA1 and EphA2, ANXA1 N-terminal 20‑30 amino acid polypeptides were synthesized in vitro, and entered into tumor cells with the help of the membrane-penetrating peptide TAT, which could significantly block the combination of ANXA1 and EphA2 in tumor cells, increase the combination of Cbl and EphA2, and promote The ubiquitination and degradation of EphA2 inhibits the growth of tumor cells in vitro and in vivo, and has a significant antitumor effect. Therefore, the EYVQTVKSSKG polypeptide can be used to prepare antitumor drugs and has important clinical application value.

Description

Technical field[0001]The invention belongs to the technical field of anti-tumor drug development and treatment, and specifically relates to an anti-tumor ANXA1 derivative polypeptide and its application.Background technique[0002]Annexins belong to the superfamily of calcium-dependent phospholipid binding proteins, which are widely present in mammals and humans, and are expressed in almost all organs. ANXA1 (Annexin 1) is the first member of this family to be identified. It has many important physiological functions such as regulation of inflammation, immunity, cell proliferation and apoptosis. Human ANXA1 protein is a cytoplasmic protein composed of 346 amino acids with a molecular weight of 37kD, which depends on the reversible binding of calcium ions to the cell membrane. It is expressed in many epithelial tissues and inflammatory cells. Initial research shows that ANXA1 has anti-inflammatory and immune regulation effects. Recent studies have found that ANXA1 is abnormally express...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C07K14/47C07K19/00A61K38/17A61P35/00
CPCA61K38/00A61P35/00C07K14/4721C07K2319/10
Inventor 肖志强冯娟卢珊珊黄伟易红肖塔
Owner XIANGYA HOSPITAL CENT SOUTH UNIV
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