NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid β

Gangliosides are targets for a variety of pathologically relevant proteins, including amyloid beta (A beta), an important component implicated in Alzheimer's disease (AD). To provide a structural basis for this pathogenic interaction associated with AD, we conducted NMR analyses of the Ab interactions with gangliosides using lyso-GM1 micelles as a model system. Our NMR data revealed that the sugar-lipid interface is primarily perturbed upon binding of A beta to the micelles, underscoring the importance of the inner part of the ganglioside cluster for accommodating A beta in comparison with the outer carbohydrate branches that provide microbial toxin-and virus-binding sites. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.