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Issue 5, 2010
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Rapid analysis of matrix metalloproteinase-3 activity by gelatin arrays using a spectral surface plasmon resonance biosensor

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Abstract

We developed a novel assay system using an array-based spectral surface plasmon resonance (SPR) biosensor for a high-throughput analysis of matrix metalloproteinase (MMP)-3 activity. Gelatin arrays were fabricated by immobilizing gelatin, a MMP-3 substrate, on amine-modified gold arrays. MMP-3 activity was determined by monitoring the shift of SPR wavelength caused by gelatin proteolysis. The gelatinolytic activity of MMP-3, which caused a decrease of the SPR wavelength, was verified by SPR spectroscopy, atomic force microscopy, and fluorescence-based protein arrays. MMP-3 activity increased by three non-ionic detergents in a dose-dependent manner, and Brij-35 was most effective. The array-based SPR biosensor was successfully applied to the rapid analysis of dose-dependent MMP-3 activity and its inhibition with tissue inhibitors of metalloproteinase 1 and GM6001, MMP inhibitors. Therefore, this new assay system using a spectral SPR biosensor is simple, label-free, and high-throughput, and is likely to have a strong potential for inhibitor screening.

Graphical abstract: Rapid analysis of matrix metalloproteinase-3 activity by gelatin arrays using a spectral surface plasmon resonance biosensor

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Publication details

The article was received on 23 Sep 2009, accepted on 26 Jan 2010 and first published on 08 Feb 2010


Article type: Paper
DOI: 10.1039/B919857A
Citation: Analyst, 2010,135, 1050-1057
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    Rapid analysis of matrix metalloproteinase-3 activity by gelatin arrays using a spectral surface plasmon resonance biosensor

    S. Jung, D. Kong, J. H. Park, S. Lee, J. Hyun, Y. Kim and K. Ha, Analyst, 2010, 135, 1050
    DOI: 10.1039/B919857A

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