Premium
Conformational Control of Integrin‐Subtype Selectivity in iso DGR Peptide Motifs: A Biological Switch
Author(s) -
Frank Andreas O.,
Otto Elke,
MasMoruno Carlos,
Schiller Herbert B.,
Marinelli Luciana,
Cosconati Sandro,
Bochen Alexander,
Vossmeyer Dörte,
Zahn Grit,
Stragies Roland,
Novellino Ettore,
Kessler Horst
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201004363
Subject(s) - pentapeptide repeat , integrin , asparagine , peptide , cyclic peptide , computational biology , chemistry , motif (music) , docking (animal) , stereochemistry , biochemistry , combinatorial chemistry , biology , medicine , amino acid , philosophy , receptor , nursing , aesthetics
The rearrangement of asparagine to isoaspartate ( iso D) is responsible for the deactivation of many functional proteins. However, the iso DGR 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.