Leveraging its dual expertise
in peptides and detection reagents, AnaSpec is pleased to announce the release
Fluor™ 750)], a labeled RGD peptide that has produced valuable
imaging in a recent in vivo research study.
Extracellular matrix proteins
containing the Arg-Gly-Asp (RGD) motif, 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 conjugate, c[RGDyK(HiLyte Fluor™ 750)], binds specifically
to some tissues in organs that are known to be rich in integrin αvβ3
(see Figure 1).
In vivo testing of this peptide labeled with an AnaSpec proprietary near infrared
fluorescent dye, HiLyte Fluor™750-labeled RGD peptide, c[RGDyK(HiLyte
Fluor™ 750)], Ex/Em = 750/780 nm, was performed by the University
of South Florida. The results were presented in a late-breaking
poster at the 20th American Peptide Symposium.
|Figure 1. In vivo fluorescent imaging of rat injected with 20 nmol
c[RGDyK(HiLyte Fluor™ 750)] conjugate 3 hours post injection.
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Additional RGD Peptides
Chen, X., P. Conti,
and R. Moats, Cancer Res. 64, 8009 (2004).