AnaSpec poster described in vivo testing of an RGD cyclic peptide labelled with a proprietary near infrared fluorescent dye, HiLyte Fluor 750-labelled RGD peptide, at 750 and 780nm
At the 2007 annual conference of the American Peptide Society, AnaSpec in collaboration with the University of South Florida presented a late-breaking technical poster that described in vivo imaging using a tissue-specific near infrared fluorescent peptide conjugate.
Extracellular matrix proteins that contain the Arg-Gly-Asp (RGD) sequence, and integrin receptors which bind this sequence, constitute a major recognition system for cell migration and adhesion processes.
In fibronectins and other proteins, the RGD binding sequence is found at the apex of a loop; such conformation has been found to allow for high affinity selectivity to integrin receptors.
Cyclic peptides have been shown to be more stable than linear peptides; in the case of RGD cyclic peptide c(RGDyK), its structure also confers increased affinity and selectivity for integrin avB3 both in cell culture and in living subjects.
Results demonstrated that in an animal model, this conjugate bound specifically to some tissues in organs that are known to be rich in integrin avB3.
