Fluorescence Detection of MMP-9. I. MMP-9 Selectively Cleaves Lys-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys Peptide

Author(s): Rafal Fudala, Amalendu P. Ranjan, Anindita Mukerjee, Jamboor K. Vishwanatha, Zygmunt Gryczynski, Julian Borejdo, Pabak Sarkar, Ignacy Gryczynski.

Journal Name: Current Pharmaceutical Biotechnology

Volume 12 , Issue 5 , 2011

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Abstract:

MMP-9 enzyme recognizes a peptide sequence Lys-Gly-Pro-Arg-Ser-Leu-Ser-Gly-Lys and cleaves the peptide into two parts. We synthesized a dual fluorophore beacon consisting of 5-FAM and Cy5 dyes. The fluorescence emission of the fluorescein moiety is dramatically quenched by Cy5 molecule due to Förster Resonance Energy Transfer (FRET) and the fluorescence of Cy5 is strongly enhanced. Upon addition of MMP-9 enzyme, the fluorescence of 5-FAM intensifies and Cy5 decreases. The control MMP-2 enzyme does not cause any changes in either 5-FAM or Cy5 fluorescence. We believe that our observation will help in early detection of elevated MMP-9 levels under disease conditions.

Keywords: MMP-9, fluorescence, FRET, labeled peptide

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Article Details

VOLUME: 12
ISSUE: 5
Year: 2011
Page: [834 - 838]
Pages: 5
DOI: 10.2174/138920111795470967
Price: $58

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