Attenuated cytotoxicity but enhanced betafibril of a mutant amyloid beta-peptide with a methionine to cysteine substitution.

Abstract:

:Amyloid-beta peptide (Abeta), the major constituent of senile plaques in the Alzheimer's disease (AD) brain, is the main source of oxidative stress leading to neurodegeneration. The methionine residue in this peptide is reported to be responsible for neurotoxicity. Structurally similar substitution with methionine 35 replaced by cysteine in Abeta(40) was synthesized, and this result in enhanced beta-sheet structures according to both circular dichroism (CD) spectra and beta-fibril specific fluorescence assay but attenuated cytotoxicity whether in the presence of copper or not. These findings may provide further evidence on disclosing the connection between amyloid beta-aggregation and Abeta-induced neurotoxicity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dai XL,Sun YX,Jiang ZF

doi

10.1016/j.febslet.2007.02.038

subject

Has Abstract

pub_date

2007-04-03 00:00:00

pages

1269-74

issue

7

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(07)00204-9

journal_volume

581

pub_type

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