Small molecule inhibitors of Abeta assembly.
The Abeta peptide assembles into a variety of distinct types of structures in vitro and in the brain which have different biological consequences. Differential effects of inhibitory small molecules suggest that a sequential monomer - oligomer - fibril mechanism is overly simplistic and that soluble toxic oligomers and fibrils can be formed in common or separate pathways depending on the local environment. As a result, the effects of inhibitors are often assay-dependent because multiple pathways are operating. This review discusses strategies for teasing apart the intricate protein-protein interactions that result in Abeta assembly.
LeVine
Harry
H
Department of Molecular and Cellular Biochemistry, Chandler School of Medicine and the Center on Aging, University of Kentucky, KY, USA. hlevine@email.uky.edu
D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D016874:Neurofibrillary Tangles / Q000737:chemistry; D017510:Protein Folding; D020836:Protein Structure, Quaternary
D016229:Amyloid beta-Peptides