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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2006-10-2
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pubmed:abstractText |
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 alphavbeta3 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 beta3 knockout cells revealed that beta3 integrin mediates the internalization of the cypate-GRD peptide. Molecular modeling studies supported preferential interaction of the probe with the beta3 subunit of integrins relative to the alphav subunit. The results demonstrate that the cypate-GRD peptide targets beta3 integrin, thereby providing a strategy to monitor drug delivery and efficacy, and physiopathologic processes mediated by this protein.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1543-8384
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
539-49
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:17009853-Animals,
pubmed-meshheading:17009853-Binding, Competitive,
pubmed-meshheading:17009853-Blotting, Western,
pubmed-meshheading:17009853-Cell Line,
pubmed-meshheading:17009853-Cell Line, Tumor,
pubmed-meshheading:17009853-Fluorescent Dyes,
pubmed-meshheading:17009853-Humans,
pubmed-meshheading:17009853-Integrin beta Chains,
pubmed-meshheading:17009853-Mice,
pubmed-meshheading:17009853-Mice, Nude,
pubmed-meshheading:17009853-Microscopy, Confocal,
pubmed-meshheading:17009853-Molecular Probes,
pubmed-meshheading:17009853-Molecular Structure,
pubmed-meshheading:17009853-Muscle, Smooth, Vascular,
pubmed-meshheading:17009853-Mutation,
pubmed-meshheading:17009853-Oligopeptides,
pubmed-meshheading:17009853-Spectroscopy, Near-Infrared,
pubmed-meshheading:17009853-Time Factors,
pubmed-meshheading:17009853-Xenograft Model Antitumor Assays
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pubmed:articleTitle |
Targeting Beta-3 integrin using a linear hexapeptide labeled with a near-infrared fluorescent molecular probe.
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pubmed:affiliation |
Department of Radiology, Washington University School of Medicine, St Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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