Length-Dependent Proteolytic Cleavage of Short Oligopeptides Catalyzed by Matrix Metalloprotease-9

被引：8

作者：

Huang, Yibing ^{[1
,2
]}

Shi, Junfeng ^{[1
]}

Yuan, Dan ^{[1
]}

Zhou, Ning ^{[1
]}

Xu, Bing ^{[1
]}

机构：

[1] Brandeis Univ, Dept Chem, Waltham, MA 02454 USA

[2] Jilin Univ, Minist Educ, Key Lab Mol Enzymol & Engn, Changchun 130012, Peoples R China

来源：

BIOPOLYMERS | 2013年 / 100卷 / 06期

关键词：

N-terminal substitution; oligopeptide; MMP-9; proteolytic sites; AROMATIC-AROMATIC INTERACTIONS; IV COLLAGENASE GELATINASE; PEPTIDE-BASED HYDROGELS; SYNTHETIC PEPTIDES; PROTEASE ACTIVITY; DESIGNED PEPTIDE; FORM NANOFIBERS; HUMAN-SKIN; IN-VIVO; CANCER;

D O I：

10.1002/bip.22240

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Matrix metalloproteinases (MMPs), as the enzymes to degrade extracellular matrix proteins, play a major role on cell behaviors. Among them, MMP-9 usually catalyzes the degradation of proteins with the dominant cleavage at G/L site. Recent high-throughput screening suggests that S/L is a new major site for the cleavage when the substrates of MMP-9 are oligopeptides. Here we examine the cleavage sites of the N-terminal substituted short oligopeptides as the substrates of MMP-9. As the first example of such study of N-substituted small peptides, our results suggest that the substitute group at the N-terminal and the length of peptides significantly affect the position of the cleavage site on the oligopeptides, which provides a useful insight for the design of small peptide derivatives as the substrates of MMP-9. (C) 2013 Wiley Periodicals, Inc.

引用

页码：790 / 795

页数：6