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Int. J. Mol. Sci. 2009, 10(3), 1314-1345; doi:10.3390/ijms10031314

Mechanism of Suppression of Protein Aggregation by α-Crystallin

1,* , 2 and 1
1 Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia 2 Oil and Gas Research Institute, Russian Academy of Sciences, Gubkina st. 3, 117971, Moscow, Russia
* Author to whom correspondence should be addressed.
Received: 30 January 2009 / Revised: 13 March 2009 / Accepted: 18 March 2009 / Published: 19 March 2009
(This article belongs to the Special Issue Protein Folding)


This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by a-crystallin, one of the small heat shock proteins. The dynamic light scattering data show that the initial stage of thermal aggregation of proteins is the formation of the initial aggregates involving hundreds of molecules of the denatured protein. Further sticking of the starting aggregates proceeds in a regime of diffusion-limited cluster-cluster aggregation. The protective effect of a-crystallin is due to transition of the aggregation process to the regime of reaction-limited cluster-cluster aggregation, wherein the sticking probability for the colliding particles becomes lower than unity.
Keywords: Chaperones; protein aggregation; α-crystallin Chaperones; protein aggregation; α-crystallin
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Markossian, K.A.; Yudin, I.K.; Kurganov, B.I. Mechanism of Suppression of Protein Aggregation by α-Crystallin. Int. J. Mol. Sci. 2009, 10, 1314-1345.

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