September 27, 2006
Journal Article

Electrochemical Proteolytic Beacon for Detection of Matrix Metalloproteinase Activities

Abstract

This communication describes a novel method for detecting of matrix metalloproteinase-7 activity using a peptide substrate labeled with a ferrocene reporter. The substrate serves as a selective ‘electrochemical proteolytic beacon’ (EPB) for this metalloproteinase. The EPB is immobilized on a gold electrode surface to enable ‘on-off’ electrochemical signaling capability for uncleaved and cleaved events. The EPB is efficiently and selectively cleaved by MMP-7 as measured by the rate of decrease in redox current of ferrocene. Direct transduction of a signal corresponding to peptide cleavage events into an electronic signal thus provides a simple, sensitive route for detecting the MMP activity. The new method allows for identification of the activity of MMP-7 in concentrations as low as 3.4 pM. The concept can be extended to design multiple peptide substrate labeled with different electroactive reporters for assaying multiple MMPs activities.

Revised: June 29, 2009 | Published: September 27, 2006

Citation

Liu G., J. Wang, D.S. Wunschel, and Y. Lin. 2006. Electrochemical Proteolytic Beacon for Detection of Matrix Metalloproteinase Activities. Journal of the American Chemical Society 128, no. 38:12382-12383. PNNL-SA-50156. doi:10.1021/ja0626638