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• W2150054723 abstract "Abstract: Integrins are cell-surface adhesion molecules involved in mediating cell–extracellular matrix interactions. High-resolution structural data are not available for these heterodimeric receptors. In order to generate tools for photoaffinity scanning of the RGD-binding site of human integrin αVβ3, new conformationally constrained ligands were designed. The ligands were based on five different cyclic peptidic or peptidomimetic scaffolds with high affinity for αVβ3. A single photoreactive group (a benzophenone moiety) was introduced at different positions relative to the RGD triad. In addition, an 125I or a biotin group was introduced as a reporting tag. Twenty-four cyclic ligands were prepared and their binding affinity for αVβ3 was determined. In most cases, the modifications resulted in a 5- to 500-fold decrease in affinity relative to the unmodified scaffold. Analogs representing three of the five families were screened for their cross-linking efficiency. Ligands with submicromolar affinities cross-linked efficiently and specifically to the integrin receptor, whereas ligands with weaker affinities gave specific cross-linking, but with lower efficiency. Almost all of the screened ligands cross-linked predominantly to the β3 subunit." @default.
• W2150054723 created "2016-06-24" @default.
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• W2150054723 date "2000-03-01" @default.
• W2150054723 modified "2023-10-02" @default.
• W2150054723 title "Design and evaluation of benzophenone-containing conformationally constrained ligands as tools for photoaffinity scanning of the integrin α_Vβ₃-ligand bimolecular interaction" @default.
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• W2150054723 doi "https://doi.org/10.1034/j.1399-3011.2000.00155.x" @default.
• W2150054723 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10727100" @default.
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