Ontology highlight
ABSTRACT:
SUBMITTER: Yagi-Utsumi M
PROVIDER: S-EPMC3034947 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Yagi-Utsumi Maho M Matsuo Koichi K Yanagisawa Katsuhiko K Gekko Kunihiko K Kato Koichi K
International journal of Alzheimer's disease 20101228
Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloid β (Aβ) to its toxic β-structured aggregates. We have previously shown that Aβ(1-40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumes α-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying the α-to-β conformational transition of Aβ on GM1 clusters, we performed spectroscopic characterization ...[more]