Mechanism of suppression of protein aggregation by α-crystallin.
This review summarizes experimental data illuminating the mechanism of suppression of heat-induced protein aggregation by alpha-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 alpha-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.
Markossian
Kira A
KA
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia.
Yudin
Igor K
IK
Oil and Gas Research Institute, Russian Academy of Sciences, Gubkina st. 3, 117971, Moscow, Russia.
Kurganov
Boris I
BI
Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia.
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D011489:Protein Denaturation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature; D038201:alpha-Crystallins / Q000737:chemistry / Q000378:metabolism*
D011506:Proteins; D038201:alpha-Crystallins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases