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Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics

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 a...

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Detalles Bibliográficos
Autores principales: Milto, Katazyna, Botyriute, Akvile, Smirnovas, Vytautas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3707827/
https://www.ncbi.nlm.nih.gov/pubmed/23874721
http://dx.doi.org/10.1371/journal.pone.0068684
Descripción
Sumario: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 [Image: see text] and [Image: see text] values at different conditions may help in better understanding influence of environmental factors on the process of fibril elongation.