Computer Simulations of Alzheimers Amyloid β-Protein Folding and Assembly

Title: Computer Simulations of Alzheimers Amyloid β-Protein Folding and Assembly

Volume: 3 Issue: 5

Author(s): Brigita Urbanc, Luis Cruz, David B. Teplow and H. Eugene Stanley

Affiliation:

Keywords: Alzheimer's disease, amyloid β-protein, computer simulations, coarse-grained protein model, protein folding, oligomer formation, fibril formation

Abstract: Pathological folding and aggregation of the amyloid β-protein (Aβ) are widely perceived as central to understanding Alzheimers disease (AD) at the molecular level. Experimental approaches to study Aβ 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 Aβ. 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.

Cite this article as:

Urbanc Brigita, Cruz Luis, Teplow B. David and Stanley H. Eugene, Computer Simulations of Alzheimers Amyloid β-Protein Folding and Assembly, Current Alzheimer Research 2006; 3 (5) . https://dx.doi.org/10.2174/156720506779025170