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Computer simulations of Alzheimer's amyloid beta-protein folding and assembly
Journal article   Open access   Peer reviewed

Computer simulations of Alzheimer's amyloid beta-protein folding and assembly

Brigita Urbanc, Luis Cruz, David B Teplow and H Eugene Stanley
Current Alzheimer research, v 3(5), pp 493-504
Dec 2006
DOI: https://doi.org/10.2174/156720506779025170
PMID: 17168648
url
https://doi.org/10.2174/156720506779025170View
Published, Version of Record (VoR)Open Access (License Unspecified),  Open

Abstract

Animals Models, Chemical Computer Simulation Humans Alzheimer Disease - metabolism Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - chemistry
Pathological folding and aggregation of the amyloid beta-protein (Abeta) are widely perceived as central to understanding Alzheimer's disease (AD) at the molecular level. Experimental approaches to study Abeta self-assembly are limited, because most relevant aggregates are quasi-stable and inhomogeneous. In contrast, simulations can provide significant insights into the problem, including specific sites in the molecule that would be attractive for drug targeting and details of the assembly pathways leading to the production of toxic assemblies. Here we review computer simulation approaches to understanding the structural biology of Abeta. We discuss the ways in which these simulations help guide experimental work, and in turn, how experimental results guide the development of theoretical and simulation approaches that may be of general utility in understanding pathologic protein folding and assembly.

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