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Amyloid-like fibril elongation follows michaelis-menten kinetics.
oleh: Katazyna Milto, Akvile Botyriute, Vytautas Smirnovas
| Format: | Article |
|---|---|
| Diterbitkan: | Public Library of Science (PLoS) 2013-01-01 |
Deskripsi
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.