Integrin α 5 β 1  Ligands: Biological Evaluation and Conformational Analysis | Zendy

Zimmermann Dunja | Zendy; Guthöhrlein Eckhart W. | Zendy; Malešević Miroslav | Zendy; Sewald Katherina | Zendy; Wobbe Lutz | Zendy; Heggemann Carolin | Zendy; Sewald Norbert | Zendy

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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 .

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