Journal
FEBS LETTERS
Volume 584, Issue 4, Pages 831-836Publisher
WILEY
DOI: 10.1016/j.febslet.2010.01.005
Keywords
Nuclear magnetic resonance; Ganglioside; Lyso-GM1; Spin label; Amyloid beta
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [20023033, 20107004]
- Japan Science and Technology Agency
- Japan Society for the Promotion of Science
- Grants-in-Aid for Scientific Research [20107004, 20023033] Funding Source: KAKEN
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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.
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