科研之友
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摘要
Because cadmium might interact with proteins and, thus, exert toxicity in organisms, it is vital to understand the molecular mechanism of the interaction between cadmium and biologically relevant proteins as well as the structural and functional changes in these proteins. In this study, the interaction between alpha-chymotrypsin (alpha-ChT) and cadmium chloride (CdCl2) was investigated by performing enzyme activity determinations, multispectroscopic measurements, isothermal titration calorimetry, and molecular docking studies. It was demonstrated that CdCl2 binds to alpha-ChT mainly via electrostatic forces with (21.0 +/- 0.982) binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosened the protein skeleton and increased the molecular volume of alpha-ChT. CdCl2 first binds to the interface of alpha-ChT and then interacts with the key residues His 57 or Asp 102 or both in the active sites, leading to the activity inhibition of alpha-ChT under the exposure of high CdCl2 concentrations.
