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Integrin α 5 β 1 Ligands: Biological Evaluation and Conformational Analysis
Author(s) -
Zimmermann Dunja,
Guthöhrlein Eckhart W.,
Malešević Miroslav,
Sewald Katherina,
Wobbe Lutz,
Heggemann Carolin,
Sewald Norbert
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400279
Subject(s) - integrin , peptide , fibronectin , cyclic peptide , chemistry , receptor , ligand (biochemistry) , computational biology , biochemistry , cell , biophysics , microbiology and biotechnology , stereochemistry , biology
Breaking up is easy . Integrin α 5 β 1 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‐β‐Ala‐), can bind α 5 β 1 with submicromolar affinity. A conformational analysis of the peptide provided information on the structural properties responsible for binding to α 5 β 1 .