Fluorescence detection of MMP-9. I. MMP-9 selectively cleaves Lys-Gly- Pro-Arg-Ser-Leu-Ser-Gly-Lys Peptide

Rafal Fudala, Amalendu P. Ranjan, Anindita Mukerjee, Jamboor K. Vishwanatha, Zygmunt Gryczynski, Julian Borejdo, Pabak Sarkar, Ignacy Gryczynski

Research output: Contribution to journalArticle

19 Scopus citations

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.

Original languageEnglish
Pages (from-to)834-838
Number of pages5
JournalCurrent Pharmaceutical Biotechnology
Volume12
Issue number5
DOIs
StatePublished - Jun 2011

Keywords

  • FRET
  • Fluorescence
  • Labeled peptide
  • MMP-9

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