2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 52(2018) N 1 p. 62-68; DOI 10.1134/S002689331801003X Full Text

A.V. Finkelstein*, N.V. Dovidchenko, O.V. Galzitskaya

Anomalous Kinetics of Amyloidogenesis Suggest a Competition between Oligomers and Fibrils

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia

Received - 2017-06-28; Accepted - 2017-08-14

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.

amyloids, kinetics, aggregation, fibril, initiation of fibril formation, amyloid aggregation half-time, fibril-catalyzed initiation, metastable oligomers, competition with amyloid formation, law of mass action