Characterization of quenched fluorescent triple helical peptides for MMP-2 and MMP-9 optical imaging

Philip P. Cheney, Gregg B. Fields, Samuel Achilefu, W. Barry Edwards

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Scopus citations

Abstract

The prevalence of the gelatinases, MMP-2 and MMP-9, in many human tumors, including breast, colorectal, prostate and gastric cancer, make them an attractive target for molecular imaging. A self assembling homotrimeric triple helical peptide (THP), incorporating sequences from type V collagen with high specificity to MMP-2 and MMP-9, was previously developed. To investigate the viability of a THP for gelatinase imaging, we conjugated 5FAM to ε-amino groups of lysine flanking the hydrolysis site and subjected this substrate (THP-5FAM) to vitro analysis. The synthesis and in vitro results was presented.

Original languageEnglish
Title of host publicationReporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications
DOIs
StatePublished - Jun 15 2009
EventReporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications - San Jose, CA, United States
Duration: Jan 26 2009Jan 29 2009

Publication series

NameProgress in Biomedical Optics and Imaging - Proceedings of SPIE
Volume7190
ISSN (Print)1605-7422

Conference

ConferenceReporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications
CountryUnited States
CitySan Jose, CA
Period01/26/0901/29/09

Keywords

  • Cancer
  • Fluorescence
  • Gelatinase
  • MMP
  • Optical imaging

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    Cheney, P. P., Fields, G. B., Achilefu, S., & Edwards, W. B. (2009). Characterization of quenched fluorescent triple helical peptides for MMP-2 and MMP-9 optical imaging. In Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications [719011] (Progress in Biomedical Optics and Imaging - Proceedings of SPIE; Vol. 7190). https://doi.org/10.1117/12.810096