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

Gangliosides are targets for a variety of pathologically relevant proteins, including amyloid beta (Abeta), 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 Abeta 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 Abeta to the micelles, underscoring the importance of the inner part of the ganglioside cluster for accommodating Abeta in comparison with the outer carbohydrate branches that provide microbial toxin- and virus-binding sites.