title: Length-dependent proteolytic cleavage of short oligopeptides catalyzed by matrix metalloprotease-9.
abstract: 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.
authors.affiliation: Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454, USA.|Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, 2599 Qianjin St., Changchun 130012, China.
authors.forename: Yibing
authors.initials: Y
authors.lastname: Huang
authors.affiliation: Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454, USA.
authors.forename: Junfeng
authors.initials: J
authors.lastname: Shi
authors.affiliation: Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454, USA.
authors.forename: Dan
authors.initials: D
authors.lastname: Yuan
authors.affiliation: Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454, USA.
authors.forename: Ning
authors.initials: N
authors.lastname: Zhou
authors.affiliation: Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454, USA.
authors.forename: Bing
authors.initials: B
authors.lastname: Xu
mesh_terms: D000595:Amino Acid Sequence; D045726:Metalloproteases; D009842:Oligopeptides / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D059748:Proteolysis
chemical_list: D009842:Oligopeptides; D010455:Peptides; D045726:Metalloproteases
keywords: MMP-9; N-terminal substitution; oligopeptide; proteolytic sites