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- Title
Switching in amyloid structure within individual fibrils: Implication for strain adaptation, species barrier and strain classification
- Authors
Baskakov, Ilia V.
- Abstract
Abstract: Amyloid fibrils are highly ordered crystal-like structures. It is generally assumed that individual amyloid fibrils consist of conformationally uniform cross-β-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.
- Subjects
PROTEIN structure; AMYLOID; FIBERS; CRYSTALS; BIOLOGICAL adaptation; PHYSIOLOGIC strain; LABORATORY mice
- Publication
FEBS Letters, 2009, Vol 583, Issue 16, p2618
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.05.044