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

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 (US)
Title of host publicationReporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications
DOIs
StatePublished - 2009
Externally publishedYes
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
Country/TerritoryUnited States
CitySan Jose, CA
Period1/26/091/29/09

Keywords

  • Cancer
  • Fluorescence
  • Gelatinase
  • MMP
  • Optical imaging

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Atomic and Molecular Physics, and Optics
  • Radiology Nuclear Medicine and imaging

Fingerprint

Dive into the research topics of 'Characterization of quenched fluorescent triple helical peptides for MMP-2 and MMP-9 optical imaging'. Together they form a unique fingerprint.

Cite this