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"Late-Breaking" Poster Presented at American Peptide Society Symposium
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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 αvβ3 both in cell culture and in living
subjects.
The AnaSpec poster described in vivo testing of an RGD cyclic peptide labeled with a
proprietary near infrared fluorescent dye, HiLyte FluorTM 750-labeled RGD
peptide, c[RGDyK(HiLyte FluorTM 750)], with excitation and emission wavelengths
at 750 and 780 nm. Results demonstrated that in an animal model, this conjugate bound
specifically to some tissues in organs that are known to be rich in integrin αvβ3.
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