1. Integrin alpha5beta1 ligands: biological evaluation and conformational analysis
- Author
-
Dunja Zimmermann, Lutz Wobbe, Carolin Heggemann, Miroslav Malesevic, Norbert Sewald, Katherina Sewald, and Eckhart W. Guthöhrlein
- Subjects
Protein Conformation ,Integrin ,Ligands ,Biochemistry ,conformation analysis ,plasmon resonance ,surface ,Humans ,Surface plasmon resonance ,Cell adhesion ,Molecular Biology ,Biological evaluation ,Integrin α5β1 ,biology ,Chemistry ,Organic Chemistry ,cell adhesion ,Surface Plasmon Resonance ,integrins ,peptides ,surface plasmon resonance ,Biophysics ,biology.protein ,Molecular Medicine ,K562 Cells ,Peptides ,Integrin alpha5beta1 - Abstract
Breaking up is easy. Integrin a5b1 is a cell-surface receptor involved in many physiological and pathological processes. Small cyclic peptides can influence the interaction between this receptor and its natural ligand, fibronectin. The peptide shown, c-(-Arg-Gly-Asp-d-Phe- Val-b-Ala-), can bind a5b1 with submicromolar affinity. A conformational analysis of the peptide provided information on the structural properties responsible for binding to a5b1.
- Published
- 2005