[摘要]：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 beta-peptide (A beta) 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 A beta(1-42). By coupling several techniques, we demonstrated that the homocysteinylation of lysine residues increase the neurotoxicity of the A beta peptide by stabilizing soluble oligomeric intermediates. Structured summary of protein interactions: A Beta 1-42 and A Beta 1-42 bind by fluorescence technology (View interaction) A Beta 1-42 and A Beta 1-42 bind by electron microscopy (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
