Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification.
Amyloid fibrils are highly ordered crystal-like structures. It is generally assumed that individual amyloid fibrils consist of conformationally uniform cross-beta-sheet structures that enable the amyloids to replicate their individual conformations via a template-dependent mechanism. Recent studies revealed that amyloids are capable of accommodating a global conformational switch from one amyloid strain to another within individual fibrils. The current review highlights the high adaptation potential of amyloid structures and discusses the implication of these findings for several emerging issues including prion strain adaptation (i.e. gradual change in strain structure). It also proposes that the catalytic activity of an amyloid structure should be separated from its templating effect, and raises the question of strain classification according to their promiscuous or species-specific nature.
Baskakov
Ilia V
IV
Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD 21201, USA. Baskakov@umbi.umd.edu
D000682:Amyloid / Q000737:chemistry* / Q000145:classification*; D000818:Animals; D008956:Models, Chemical; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation
D000682:Amyloid; D011328:Prions