Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.
The discovery of prion disease and the establishment of the protein only hypothesis of prion propagation raised substantial interest in the class of maladies referred to as conformational diseases. Although significant progress has been made in elucidating the mechanisms of polymerization for several amyloidogenic proteins and peptides linked to conformational disorders and solving their fibrillar 3D structures, studies of prion protein amyloid fibrils and their polymerization mechanism have proven to be very difficult. The present minireview introduces the mechanism of branched-chain reaction for describing the peculiar kinetics of prion polymerization and summarizes our current knowledge about the substructure of prion protein amyloid fibrils.
Baskakov
Ilia V
IV
Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA. baskakov@umbi.umd.edu
D000682:Amyloid / Q000378:metabolism* / Q000648:ultrastructure*; D000818:Animals; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D011328:Prions / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D011485:Protein Binding; D011487:Protein Conformation
D000682:Amyloid; D001704:Biopolymers; D011328:Prions