[Anomalous Kinetics of Amyloidogenesis Suggest a Competition between Oligomers and Fibrils]

Mol Biol (Mosk). 2018 Jan-Feb;52(1):73-81. doi: 10.7868/S002689841801010X.
[Article in Russian]


Meisl et al. have recently observed an anomalous dependence of the amyloid formation rate on the protein concentration. A novel mechanism of fibril growth has been proposed by Meisl et al. to explain the abnormality; it consists in the fibril-catalyzed initiation of fibril formation with saturation of catalytic sites at high concentrations of substrates. Our article describes an alternative explanation of the anomalous kinetics, assuming that the formation of metastable oligomers competes with fibril formation by decreasing the concentration of free monomers. Oligomers are indeed observed in the course of amyloid formation, but are usually considered as seeds of amyloid fibrils rather as their competitors. However, the oligomers visually detectable by electron microscopy were shown to be close in size to those that can be derived from the anomalous dependence of the amyloid growth rate on the protein concentration, given that the anomaly results from competition between oligomer formation and amyloidogenesis.

Keywords: aggregation; amyloid aggregation half-time; amyloids; competition with amyloid formation; fibril; fibril-catalyzed initiation; initiation of fibril formation; kinetics; law of mass action; metastable oligomers.

MeSH terms

  • Amyloid / chemistry*
  • Amyloid / ultrastructure
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / ultrastructure
  • Kinetics


  • Amyloid
  • Amyloid beta-Peptides