A fusion peptide regulating stat3 phosphorylation and its application

A technology of phosphorylation and fusion of peptides, applied in the field of biomedicine, can solve problems such as application limitations, and achieve the effects of good transmembrane activity, inhibition of inflammatory response, and inhibition of activation

Inactive Publication Date: 2017-01-04
XI AN JIAOTONG UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] Biological macromolecules play an important role in the treatment of many diseases, and due to the natural barrier function of the cell membrane, the application of such macromolecules with therapeutic value but no cell membrane penetration in cell biology, pharmacy and clinical treatment is greatly improved. restricted

Method used

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  • A fusion peptide regulating stat3 phosphorylation and its application
  • A fusion peptide regulating stat3 phosphorylation and its application
  • A fusion peptide regulating stat3 phosphorylation and its application

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Experimental program
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Embodiment Construction

[0039] 1. Chemically synthesized fusion peptide

[0040] The fusion peptide TAT-KIR was synthesized by Shanghai Chueptide Biotechnology Co., Ltd., wherein the KIR polypeptide sequence is: L-K-T-F-S-S-K-S-E-Y-Q-L, and the TAT sequence is: R-K-K-R-R-Q-R-R-R. The fusion peptide is N-terminally labeled with fluorescein isothiocyanate (FITC).

[0041] In order to reduce the molecular weight of the target peptide and increase the membrane-penetrating efficiency of the membrane-penetrating peptide, a part of the sequence truncated from the SOCS3 protein was selected as the KIR. After screening, the KIR similar to the JAK activation loop of the JAK substrate can be used as a false substrate to prevent the combination of the JAK substrate and JAK, thereby inhibiting the activity of JAK, thereby inhibiting the activation of the JAK / STAT3 signaling pathway and inhibiting the inflammatory response .

[0042] 2. Detection of fusion peptide transmembrane transport efficiency

[0043] PC12...

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Abstract

The invention discloses a fusion peptide for regulating and controlling expression of a phosphorylated STAT3 (Signal Transducer and Activator 3 of Transcription). The fusion peptide is based on a TAT (Transducer and Activator of Transcription) sequence of a cell-penetrating peptide and a kinase inhibition region (KIR) sequence of a cell factor signal transduction inhibiting factor 3; the amino terminal of the fusion peptide is marked by using fluorescein isothiocyanate (FITC). The nucleotide sequence of the fusion peptide is as shown in SEQ ID NO.3. The fusion peptide shown in SEQ ID NO.3 can be applied to regulation and control of the expression of the phosphorylated STAT3 or is applied as a novel treating target for inhibiting inflammatory reaction and promoting damage repair.

Description

[0001] Technical field: [0002] The invention belongs to the field of biomedicine and relates to the artificial design and synthesis of biologically active polypeptides, in particular to a fusion peptide regulating STAT3 phosphorylation and its application. [0003] Background technique: [0004] 1. Research progress of cytokine signal transduction inhibitor 3 kinase inhibitory region (KIR) [0005] As an important inhibitor of cytokine signal transduction pathway, suppressor of cytokine signal transduction 3 (SOCS3) can specifically inhibit the JAK / STAT3 signaling pathway mediated by inflammatory factors, forming a negative feedback regulation of JAK / STAT3 pathway, It plays a key role in curbing the inflammatory response, so it is considered to be the most potential therapeutic target to improve the repair effect of inflammatory damage. [0006] SOCS3 usually negatively regulates the JAK / STAT3 signaling pathway through the following three pathways: (1) The SH2 domain similar...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C07K19/00A61K38/16A61P9/10A61P29/00
Inventor 吕海侠王丽马辉焦倩燕晗祺马雯张智超刘勇
Owner XI AN JIAOTONG UNIV
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