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NMR characterization of the interactions between lyso‐GM1 aqueous micelles and amyloid β
Author(s) -
Yagi-Utsumi Maho,
Kameda Tomoshi,
Yamaguchi Yoshiki,
Kato Koichi
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.01.005
Subject(s) - lyso , chemistry , micelle , amyloid (mycology) , characterization (materials science) , aqueous solution , biophysics , organic chemistry , nanotechnology , materials science , biology , inorganic chemistry , scintillator , detector , electrical engineering , engineering
Gangliosides are targets for a variety of pathologically relevant proteins, including amyloid β (Aβ), 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 Aβ 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 Aβ to the micelles, underscoring the importance of the inner part of the ganglioside cluster for accommodating Aβ in comparison with the outer carbohydrate branches that provide microbial toxin‐ and virus‐binding sites.