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- W2106467306 abstract "Biomolecules containing the RGD peptide sequence are known to bind integrins with high affinity. Studies of hexa-and hepta-peptides labeled with a near-infrared fluorescent probe (cypate) showed that rearranging the glycine in a linear RGD peptide sequence to form the GRD analogue favored the uptake of the GRD compound by αvβ3 integrin receptor (ABIR)-positive A549 tumor cells and tissue. The internalization of the GRD compound in A549 cells and tumor uptake in mice were inhibited by ABIR-avid peptides, suggesting its recognition by this receptor. Further studies with functional blocking antibodies and β3 knockout cells revealed that β3 integrin mediates the internalization of the cypate-GRD peptide. Molecular modeling studies supported preferential interaction of the probe with the β3 subunit of integrins relative to the αv subunit. The results demonstrate that the cypate-GRD peptide targets β3 integrin, thereby providing a strategy to monitor drug delivery and efficacy, and physiopathologic processes mediated by this protein. Keywords: Integrin; cancer; near-infrared; imaging; molecular probe" @default.
- W2106467306 created "2016-06-24" @default.
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- W2106467306 date "2006-08-29" @default.
- W2106467306 modified "2023-09-28" @default.
- W2106467306 title "Targeting Beta-3 Integrin Using a Linear Hexapeptide Labeled with a Near-Infrared Fluorescent Molecular Probe" @default.
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- W2106467306 doi "https://doi.org/10.1021/mp0600642" @default.
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