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Interaction between amyloid β‐protein aggregates and membranes
Author(s) -
Kakio Atsuko,
Yano Yoshiaki,
Takai Denshi,
Kuroda Yukihiro,
Matsumoto Osamu,
Kozutsumi Yasunori,
Matsuzaki Katsumi
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.570
Subject(s) - membrane , chemistry , biophysics , amyloid (mycology) , thioflavin , protein aggregation , sphingomyelin , biochemistry , alzheimer's disease , biology , medicine , inorganic chemistry , disease , pathology
The conversion of soluble, nontoxic amyloid β‐protein (Aβ) to aggregated, toxic Aβ rich in β‐sheet structures is considered to be the key step in the development of Alzheimer's disease. Therefore, extensive studies have been carried out on the mechanisms involved in Aβ aggregation and the characterization of Aβ aggregates formed in aqueous solutions mimicking biological fluids. On the other hand, several investigators pointed out that membranes play an important role in Aβ aggregation. However, it remains unclear whether Aβ aggregates formed in solution and membranes are identical and whether the former can bind to membranes. In this study, using a dye‐labeled Aβ‐(1–40) as well as native Aβ‐(1–40), the properties of Aβ aggregates formed in buffer and raft‐like membranes composed of monosialoganglioside GM1/cholesterol/sphingomyelin were compared. Fourier transform infrared spectroscopic measurements suggested that Aβ aggregates formed in buffer and in membranes have different β‐sheet structures. Fluorescence experiments revealed that Aβ aggregated in buffer did not show any affinity for membranes. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.