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Attenuated cytotoxicity but enhanced βfibril of a mutant amyloid β‐peptide with a methionine to cysteine substitution
Author(s) -
Dai Xue-Ling,
Sun Ya-Xuan,
Jiang Zhao-Feng
Publication year - 2007
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.2007.02.038
Subject(s) - neurotoxicity , peptide , cytotoxicity , chemistry , methionine , senile plaques , neurodegeneration , cysteine , amyloid (mycology) , circular dichroism , fibril , biochemistry , biophysics , alzheimer's disease , amino acid , in vitro , toxicity , biology , medicine , pathology , disease , organic chemistry , enzyme , inorganic chemistry
Amyloid‐β peptide (Aβ), 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 Aβ 40 was synthesized, and this result in enhanced β‐sheet structures according to both circular dichroism (CD) spectra and β‐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 β‐aggregation and Aβ‐induced neurotoxicity.