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. 2013 Nov;100(6):790-795.
doi: 10.1002/bip.22240.

Length-dependent proteolytic cleavage of short oligopeptides catalyzed by matrix metalloprotease-9

Yibing Huang #  1   2 , Junfeng Shi #  1 , Dan Yuan  1 , Ning Zhou  1 , Bing Xu  1
Affiliations

Length-dependent proteolytic cleavage of short oligopeptides catalyzed by matrix metalloprotease-9

Yibing Huang et al. Biopolymers. 2013 Nov.

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.

Keywords: MMP-9; N-terminal substitution; oligopeptide; proteolytic sites.

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Figures

Figure 1
Figure 1
The oligopeptide sequences and the experimentally determined cleavage sites when they are treated by MMP-9 (the large arrows indicate the major cleavage sites).
Figure 2
Figure 2
The histogram of the percentage of the hydrolysis products from the oligopeptides (containing the G/L site) incubated with MMP-9 for 6 h and 72 h. The red bar shows the percentage of the remaining substrate, the other bars show the percentage of the N-substituted products due to the cleavage at the indicated site.
Figure 3
Figure 3
The histogram of the percentage of the hydrolysis products from the oligopeptides (containing the S/L site) incubated with MMP-9 for 6 h and 72 h. The red bar shows the percentage of the remaining substrate, the other bars show the percentage of the N-substituted products due to the cleavage at the indicated site.
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