title: Filming protein fibrillogenesis in real time.
abstract: Protein fibrillogenesis is a universal tool of nano-to-micro scale construction supporting different forms of biological function. Its exploitable potential in nanoscience and technology is substantial, but the direct observation of homogeneous fibre growth able to underpin a kinetic-based rationale for building customized nanostructures in situ is lacking. Here we introduce a kinetic model of de novo protein fibrillogenesis which we imaged at the nanoscale and in real time, filmed. The model helped to reveal that, in contrast to heterogeneous amyloid assemblies, homogeneous protein recruitment is principally characterized by uniform rates of cooperative growth at both ends of growing fibers, bi-directional growth, with lateral growth arrested at a post-seeding stage. The model provides a foundation for in situ engineering of sequence-prescribed fibrous architectures.
authors.affiliation: National Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
authors.forename: Angelo
authors.initials: A
authors.lastname: Bella
authors.affiliation: National Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
authors.forename: Michael
authors.initials: M
authors.lastname: Shaw
authors.affiliation: National Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK.
authors.forename: Santanu
authors.initials: S
authors.lastname: Ray
authors.affiliation: 1] National Physical Laboratory, Hampton Road, Teddington, TW11 0LW, UK [2] School of Physics and Astronomy, University of Edinburgh, UK EH9 3JZ, UK.
authors.forename: Maxim G
authors.initials: MG
authors.lastname: Ryadnov
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D007700:Kinetics; D049329:Nanostructures / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000682:Amyloid