Effect of N-homocysteinylation on physicochemical and cytotoxic properties of amyloid β-peptide.

Abstract:

:Abstract Hyperhomocysteinemia has recently been identified as an important risk factor for Alzheimer's disease (AD). One of the potential mechanisms underlying harmful effects of homocysteine (Hcy) is site-specific acylation of proteins at lysine residues by homocysteine thiolactone (HCTL). The accumulation of amyloid β-peptide (Aβ) in the brain is a neuropathological hallmark of AD. In the present study we were interested to investigate the effects of N-homocysteinylation on the aggregation propensity and neurotoxicity of Aβ(1-42). By coupling several techniques, we demonstrated that the homocysteinylation of lysine residues increase the neurotoxicity of the Aβ peptide by stabilizing soluble oligomeric intermediates.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Khodadadi S,Riazi GH,Ahmadian S,Hoveizi E,Karima O,Aryapour H

doi

10.1016/j.febslet.2011.12.018

subject

Has Abstract

pub_date

2012-01-20 00:00:00

pages

127-31

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00890-8

journal_volume

586

pub_type

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