Probing for Integrin v3 Bin
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- 作者：Wei Wang ; Qingping Wu ; Marites Pasuelo ; John S. McMurray ; and Chun Li
- 刊名：Bioconjugate Chemistry
- 出版年：2005
- 出版时间：May 2005
- 年：2005
- 卷：16
- 期：3
- 页码：729 - 734
- 全文大小：125K
- 年卷期：v.16,no.3(May 2005)
- ISSN：1520-4812
文摘
Integrin 
v
3 is an adhesion molecule involved in tumor invasion, angiogenesis, and metastasis. Thereis substantial interest in developing novel agents that bind to integrin v3. Here we report thesynthesis and characterization of a fluorescent integrin v3 probe and its use in a nonradioactive,simple, sensitive fluorescence polarization (FP) assay to quantify binding to integrin v3. For assayvalidation, the FP assay was compared to a cell adhesion assay. In the two assays, probe binding tointegrin v3 showed a similar dependence on probe concentration. The FP assay was successfullyapplied to measure the binding affinity to integrin v3 of several cyclic peptides containing the Arg-Gly-Asp (RGD) motif. The FP assay we describe here may be appropriate for high-throughput screeningfor integrin v3-binding ligands used for anti-integrin therapy or noninvasive imaging of integrinexpression.
v3 is an adhesion molecule involved in tumor invasion, angiogenesis, and metastasis. Thereis substantial interest in developing novel agents that bind to integrin v3. Here we report thesynthesis and characterization of a fluorescent integrin v3 probe and its use in a nonradioactive,simple, sensitive fluorescence polarization (FP) assay to quantify binding to integrin v3. For assayvalidation, the FP assay was compared to a cell adhesion assay. In the two assays, probe binding tointegrin v3 showed a similar dependence on probe concentration. The FP assay was successfullyapplied to measure the binding affinity to integrin v3 of several cyclic peptides containing the Arg-Gly-Asp (RGD) motif. The FP assay we describe here may be appropriate for high-throughput screeningfor integrin v3-binding ligands used for anti-integrin therapy or noninvasive imaging of integrinexpression.