Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Yoshiko Miura; Chouga You; Reiko Ohnishi

doi:10.1088/1468-6996/9/2/024407

Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Yoshiko Miura, Chouga You, Reiko Ohnishi

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

A glycopolymer carrying trehalose was found to suppress the formation of amyloid fibrils from the amyloid β peptide (1-42) (Aβ), as evaluated by thioflavin T assay and atomic force microscopy. Glycopolymers carrying sugar alcohols also changed the aggregation properties of Aβ, and the inhibitory effect depended on the type of sugar and alkyl side chain. Neutralization activity was confirmed by in vitro assay using HeLa cells. The glycopolymer carrying trehalose strongly inhibited amyloid formation and neutralized cytotoxicity.

Original language	English
Article number	024407
Journal	Science and Technology of Advanced Materials
Volume	9
Issue number	2
DOIs	https://doi.org/10.1088/1468-6996/9/2/024407
Publication status	Published - Apr 1 2008
Externally published	Yes

All Science Journal Classification (ASJC) codes

Materials Science(all)

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10.1088/1468-6996/9/2/024407

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AB - A glycopolymer carrying trehalose was found to suppress the formation of amyloid fibrils from the amyloid β peptide (1-42) (Aβ), as evaluated by thioflavin T assay and atomic force microscopy. Glycopolymers carrying sugar alcohols also changed the aggregation properties of Aβ, and the inhibitory effect depended on the type of sugar and alkyl side chain. Neutralization activity was confirmed by in vitro assay using HeLa cells. The glycopolymer carrying trehalose strongly inhibited amyloid formation and neutralized cytotoxicity.

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Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Abstract

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