title: Stop-and-go kinetics in amyloid fibrillation.
abstract: Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.
authors.affiliation: DTU Elektro, Building 349, Ørsteds Plads, Technical University of Denmark, 2800 Lyngby, Denmark. jfb@elektro.dtu.dk
authors.forename: Jesper
authors.initials: J
authors.lastname: Ferkinghoff-Borg
authors.forename: Jesper
authors.initials: J
authors.lastname: Fonslet
authors.forename: Christian Beyschau
authors.initials: CB
authors.lastname: Andersen
authors.forename: Sandeep
authors.initials: S
authors.lastname: Krishna
authors.forename: Simone
authors.initials: S
authors.lastname: Pigolotti
authors.forename: Hisashi
authors.initials: H
authors.lastname: Yagi
authors.forename: Yuji
authors.initials: Y
authors.lastname: Goto
authors.forename: Daniel
authors.initials: D
authors.lastname: Otzen
authors.forename: Mogens H
authors.initials: MH
authors.lastname: Jensen
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D046912:Multiprotein Complexes