Imaging of αvβ3 Expression by a Bifunctional Chimeric RGD Peptide not Cross-Reacting with αvβ5
نویسندگان
چکیده
منابع مشابه
A new cyclic RGD peptide dimer for integrin αvβ3 imaging.
OBJECTIVE To design a new Arg-Gly-Asp (RGD) peptide that can specifically bind integrin αvβ3 and evaluate the possibility of using 131I-labeled peptide for imaging αvβ3-positive tumors. MATERIALS AND METHODS The structure of the RGD monomer was selected using V-life software. Based on the RGD monomer, a dimer of cyclic RGD [c(RGD)2] linked by Tyr-(D)Ser-Lys-(D)Ser-Ser with a Gly-Gly-(D)Ala-Gl...
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This study sought to evaluate FITC-conjugated cyclic RGD peptides (FITC-RGD2, FITC-3P-RGD2, and FITC-Galacto-RGD2) as fluorescent probes for in vitro assays of integrin αvβ3/αvβ5 expression in tumor tissues. FITC-RGD2, FITC-3P-RGD2, and FITC-Galacto-RGD2 were prepared, and their integrin αvβ3/αvβ5 binding affinity was determined using the displacement assay against (125)I-echistatin bound to U8...
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BACKGROUND Hybrid PET/optical imaging provides quantitative and complementary information for diagnosis of tumors. Herein, we developed a (64)Cu-labeled AlexaFluor 680-streptavidin ((AF)SAv)/biotin-based dimeric cyclic RGD peptide (RGD2) for hybrid PET/optical imaging of integrin αVβ3 expression. METHODS (64)Cu-1,4,7,10-tetraazacyclododecane-N,N',N'',N'''-tetraacetic acid (DOTA)-(AF)SAv/bioti...
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Syndecan-1 (Sdc1) is a matrix receptor shown to associate via its extracellular domain with the alpha(v)beta(3) and alpha(v)beta(5) integrins, potentially regulating cell adhesion, spreading, and invasion of cells expressing these integrins. Using Sdc1 deletion mutants expressed in human mammary carcinoma cells, we identified the active site within the Sdc1 core protein and derived a peptide in...
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Ligand-protein interactions have been recognized as central phenomena in most biological processes ranging from catalysis to signaling . Theoretical and computational methods are widely used to analyze, investigate, and predict ligand-macromolecule interactions. In order to better understand the structural requirements of Integrins-ligand binding a series of RGD analogues were examined using do...
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ژورنال
عنوان ژورنال: Clinical Cancer Research
سال: 2009
ISSN: 1078-0432,1557-3265
DOI: 10.1158/1078-0432.ccr-08-3270