Conformational Control of Integrin-Subtype Selectivity in isoDGR Peptide Motifs: A Biological Switch (pages 9278–9281)
Dr. Andreas O. Frank, Dipl.-Chem. Elke Otto, Dr. Carlos Mas-Moruno, Dr. Herbert B. Schiller, Prof. Dr. Luciana Marinelli, Dr. Sandro Cosconati, Dipl.-Chem. Alexander Bochen, Dr. Dörte Vossmeyer, Dr. Grit Zahn, Dr. Roland Stragies, Prof. Dr. Ettore Novellino and Prof. Dr. Horst Kessler
Version of Record online: 18 OCT 2010 | DOI: 10.1002/anie.201004363
The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to α5β1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide.