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Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics

Author

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  • Katazyna Milto
  • Akvile Botyriute
  • Vytautas Smirnovas

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 and values at different conditions may help in better understanding influence of environmental factors on the process of fibril elongation.

Suggested Citation

  • Katazyna Milto & Akvile Botyriute & Vytautas Smirnovas, 2013. "Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics," PLOS ONE, Public Library of Science, vol. 8(7), pages 1-5, July.
    • Handle: RePEc:plo:pone00:0068684
    DOI: 10.1371/journal.pone.0068684
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    References listed on IDEAS

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    1. Gabriela P. Saborio & Bruno Permanne & Claudio Soto, 2001. "Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding," Nature, Nature, vol. 411(6839), pages 810-813, June.
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    1. Ricardas Malisauskas & Akvile Botyriute & Jonathan G Cannon & Vytautas Smirnovas, 2015. "Flavone Derivatives as Inhibitors of Insulin Amyloid-Like Fibril Formation," PLOS ONE, Public Library of Science, vol. 10(3), pages 1-14, March.

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