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Length‐dependent proteolytic cleavage of short oligopeptides catalyzed by matrix metalloprotease‐9
Author(s) -
Huang Yibing,
Shi Junfeng,
Yuan Dan,
Zhou Ning,
Xu Bing
Publication year - 2013
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22240
Subject(s) - cleavage (geology) , oligopeptide , chemistry , matrix metalloproteinase , peptide , extracellular matrix , enzyme , metalloproteinase , extracellular , biochemistry , stereochemistry , biology , paleontology , fracture (geology)
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. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 790–795, 2013.