Synthesis, Chemical Characterization and Multiscale Biological Evaluation of a Dimeric-cRGD Peptide for Targeted Imaging of α _V β ₃ Integrin Activity.

ABSTRACT: Cyclic peptides containing the Arg-Gly-Asp (RGD) sequence have been shown to specifically bind the angiogenesis biomarker α _V β ₃ integrin. We report the synthesis, chemical characterization, and biological evaluation of two novel dimeric cyclic RGD-based molecular probes for the targeted imaging of α _V β ₃ activity (a radiolabeled version, ⁶⁴Cu-NOTA-PEG₄-cRGD₂, for PET imaging, and a fluorescent version, FITC-PEG₄-cRGD₂, for in vitro work). We investigated the performance of this probe at the receptor, cell, organ, and whole-body levels, including its use to detect diabetes associated impairment of ischemia-induced myocardial angiogenesis. Both versions of the probe were found to be stable,

SUBMITTER: Hedhli J 

PROVIDER: S-EPMC5466598 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature