Crosslinking of amyloid-β peptide to brain acetylcholinesterase

Abstract
Acetylcholinesterase (AChE) is the enzyme responsible for the hydrolysis of the neurotransmitter acetylcholine in the central nervous system. Recently, we have found that AChE promotes the assembly of amyloid-β peptides (Aβ) into Alzheimer fibrils. The action of AChE on the state of aggregation of the Aβ peptide supposes a near neighbor relationship between these two molecules. In the present work, we have studied Aβ-AChE interactions using the crosslinker reagent disuccinimidyl suberate (DSS), in the presence of [125I]-Aβ peptide. The Aβ-AChE complexes formed by crosslinking were then analyzed by SDS-PAGE and autoradiography. We observed the formation of [125I] Aβ-labeled complexes of 70, 160, 250, and 300 kDa corresponding to monomers, dimers, tetramers, and oligomers of AChE, respectively crosslinked with the Aβ peptide. Our results suggest that AChE and the Aβ peptide may be involved in physiologically relevant interactions, related to the pathogenesis of Alzheimer disease (AD).

This publication has 33 references indexed in Scilit: