title: A clear view of polymorphism, twist, and chirality in amyloid fibril formation.
abstract: The self-assembly of protein molecules into highly ordered linear aggregates, known as amyloid fibrils, is a phenomenon receiving increasing attention because of its biological roles in health and disease and the potential of these structures to form artificial proteinaceous scaffolds for biomaterials applications. A particularly powerful approach to probe the key physical properties of fibrillar structures is atomic force microscopy, which was used by Usov et al. in this issue of ACS Nano to reveal the polymorphic transitions and chirality inversions of amyloid fibrils in unprecedented detail. Starting from this study, this Perspective highlights recent progress in understanding the dynamic polymorphism, twisting behavior, and handedness of amyloid fibrils and discusses the promising future of these self-assembling structures as advanced functional materials with applications in nanotechnology and related fields.
authors.affiliation: Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, United Kingdom.
authors.forename: Lisa R
authors.initials: LR
authors.lastname: Volpatti
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
authors.forename: Tuomas P J
authors.initials: TP
authors.lastname: Knowles
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry*
chemical_list: D000682:Amyloid; D012710:Serum Albumin, Bovine