Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide

Abstract

Background: Binding of Dab2 to sulfatides results in platelet aggregation inhibition. Results: The structure of a Dab2-derived peptide (SBM) embedded in dodecylphosphocholine micelles, characterization of its minimal functional sulfatide-binding site, and its inhibitory platelet aggregation activity were determined. Conclusion: An amphipathic helical region of Dab2 SBM binds sulfatides, leading to platelet aggregation inhibition. Significance: Dab2 SBM may lead to the design of novel aggregatory inhibitors. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.