title: Understanding protein aggregation from the view of monomer dynamics.
abstract: Much work in recent years has been devoted to understanding the complex process of protein aggregation. This review looks at the earliest stages of aggregation, long before the formation of fibrils that are the hallmark of many aggregation-based diseases, and proposes that the first steps are controlled by the reconfiguration dynamics of the monomer. When reconfiguration is much faster or much slower than bimolecular diffusion, then aggregation is slow, but when they are similar, aggregation is fast. The experimental evidence for this model is reviewed and the prospects for small molecule aggregation inhibitors to prevent disease are discussed.
authors.affiliation: Department of Physics and Astronomy and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. lapidus@msu.edu
authors.forename: Lisa J
authors.initials: LJ
authors.lastname: Lapidus
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000682:Amyloid; D021122:Protein Subunits; D011506:Proteins