Jump to main content
Jump to site search

Issue 1, 2016
Previous Article Next Article

Peptide microarray-based fluorescence assay for simultaneously detecting matrix metalloproteinases

Author affiliations

Abstract

Matrix metalloproteinases (MMPs) are believed to play an important role in tumor invasion. Herein, a peptide microarray-based fluorescence assay has been proposed for simultaneously determining the activities of MMP-2 and MMP-9 through the strong binding affinity of fluorescein isothiocyanate modified avidin (avidin-FITC) with the immobilized biotinylated peptide substrate on the microarray. In the presence of MMPs, the biotin moiety is released from the microarray by enzymatic cleavage of the peptide substrate, resulting in a significant decrease of the fluorescence signal. Under the optimal experimental conditions, the fluorescence intensity changes (ΔF%) are proportional to the concentrations of MMP-2 and MMP-9 within the ranges of 50 pg mL−1 to 50 ng mL−1 and 50 pg mL−1 to 100 ng mL−1 in the enzyme mixture, respectively. The detection limits are 45 pg mL−1 for MMP-2, and 60 pg mL−1 for MMP-9. In particular, the activities of extracellular MMP-2 and MMP-9 are determined by the peptide microarray-based fluorescence assay, and satisfactory results are obtained.

Graphical abstract: Peptide microarray-based fluorescence assay for simultaneously detecting matrix metalloproteinases

Back to tab navigation

Supplementary files

Publication details

The article was received on 03 Aug 2015, accepted on 06 Sep 2015 and first published on 08 Sep 2015


Article type: Paper
DOI: 10.1039/C5AY02041G
Anal. Methods, 2016,8, 72-77

  •   Request permissions

    Peptide microarray-based fluorescence assay for simultaneously detecting matrix metalloproteinases

    Z. Lei, J. Gao, X. Liu, D. Liu and Z. Wang, Anal. Methods, 2016, 8, 72
    DOI: 10.1039/C5AY02041G

Search articles by author

Spotlight

Advertisements