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Localization of amyloid beta (Aβ1‐42) protofibrils in membrane lateral compartments: Effect of cholesterol and 7‐Ketocholesterol
Author(s) -
Phan Huong T.T.,
Vestergaard Mun'delanji C.,
Baek KeangOk,
Shimokawa Naofumi,
Takagi Masahiro
Publication year - 2014
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.2014.08.007
Subject(s) - membrane , cholesterol , chemistry , biophysics , peptide , membrane fluidity , amyloid (mycology) , cell membrane , biochemistry , biology , inorganic chemistry
Cholesterol plays an important role in the interaction of Alzheimer's amyloid beta (Aβ) with cell membranes, an important event in Aβ‐induced cytotoxicity. However, it is not fully understood how cholesterol influences the association of Aβ with membrane lateral compartments. We have shown that by modulating membrane fluidity, cholesterol decreased peptide localization in solid‐ordered domains and increased that in liquid‐ordered domains. It changed the amount of Aβ associating with liquid‐disordered (Ld) phase with different tendencies depending on the composition of heterogeneous membrane systems. 7‐Ketocholesterol, an oxidized derivative of cholesterol, majorly enhanced the fluidity of and Aβ interaction with Ld phase. These findings are useful for clarifying the impact of cholesterol and its oxidation in Aβ‐induced toxicity.