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• W2077639460 abstract "The ICAM-1 adhesion molecule is expressed selectively at low levels on endothelial cells but is strongly upregulated in dysfunctional endothelial cells associated with inflammation, cancer, and atherogenesis. Using COS-7 cells transfected with murine ICAM-1 (mICAM-1) as a target receptor, a phage display library was screened. Clones were selected by elution with a mAb specific for a functional epitope of ICAM-1 and a novel peptide sequence binding to the extracellular domain of mICAM-1 was identified that can potentially be used as a targeting vector aimed at dysfunctional endothelium. We further showed that the targeting specificity of the peptide was retained following its incorporation at the N terminal end of a large chimeric protein. Moreover, this chimeric protein containing the mICAM-1-specific sequence was found to inhibit ICAM-1-mediated intercellular adhesion during antigen presentation. Taken together, these results demonstrate the potential for improving the cell-selectivity and properties of therapeutical agents toward targeting adhesion molecules involved in cell–cell interactions." @default.
• W2077639460 created "2016-06-24" @default.
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• W2077639460 date "2003-09-01" @default.
• W2077639460 modified "2023-10-16" @default.
• W2077639460 title "Identification of a murine ICAM-1-specific peptide by subtractive phage library selection on cells" @default.
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• W2077639460 doi "https://doi.org/10.1016/j.bbrc.2003.08.050" @default.
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