title: Amyloid-like fibril elongation follows michaelis-menten kinetics.
abstract: A number of proteins can aggregate into amyloid-like fibrils. It was noted that fibril elongation has similarities to an enzymatic reaction, where monomers or oligomers would play a role of substrate and nuclei/fibrils would play a role of enzyme. The question is how similar these processes really are. We obtained experimental data on insulin amyloid-like fibril elongation at the conditions where other processes which may impact kinetics of fibril formation are minor and fitted it using Michaelis-Menten equation. The correlation of the fit is very good and repeatable. It speaks in favour of enzyme-like model of fibril elongation. In addition, obtained [Formula: see text] and [Formula: see text] values at different conditions may help in better understanding influence of environmental factors on the process of fibril elongation.
authors.affiliation: Department of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology, Vilnius, Lithuania.
authors.forename: Katazyna
authors.initials: K
authors.lastname: Milto
authors.forename: Akvile
authors.initials: A
authors.lastname: Botyriute
authors.forename: Vytautas
authors.initials: V
authors.lastname: Smirnovas
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects / Q000648:ultrastructure; D019220:High-Energy Shock Waves; D006801:Humans; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D046529:Microscopy, Electron, Transmission; D055503:Protein Multimerization / Q000187:drug effects / Q000502:physiology* / Q000528:radiation effects; D012965:Sodium Chloride / Q000494:pharmacology; D013010:Sonication
chemical_list: D000682:Amyloid; D007328:Insulin; D012965:Sodium Chloride