Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. e68684

Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. e68684

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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Veröffentlicht in:PloS one 2013-07, Vol.8 (7)
Hauptverfasser: Milto, Katazyna, Botyriute, Akvile, Smirnovas, Vytautas
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Environmental factors
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Smirnovas, Vytautas
description 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 and values at different conditions may help in better understanding influence of environmental factors on the process of fibril elongation.
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title Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. e68684
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