Abstract
The study of the kinetics of thermal aggregation of glycogen phosphorylase b (Phb) from rabbit skeletal muscles by dynamic light scattering at 48°C showed that 2-hydroxypropyl-β-cyclodextrin (HP-β-CD) accelerated the aggregation process and induced the formation of the larger protein aggregates. The reason of the accelerating effect of HP-β-CD is destabilization of the protein molecule under action of HP-β-CD. This conclusion was supported by the data on differential scanning calorimetry and the kinetic data on thermal inactivation of Phb. It is assumed that destabilization of the Phb molecule is due to preferential binding of HP-β-CD to intermediates of protein unfolding in comparison with the original native state. The conclusion regarding the ability of the native Phb for binding of HP-β-CD was substantiated by the data on the enzyme inhibition by HP-β-CD. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 986-993, 2010.
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