Physicochemical properties of the antitumor ribonucleases

Here, the homology modeling approach was used to predict the three-dimensional structure of ribonuclease from Bacillus circulans (Bci-RNase), B. coagulans (Bco-RNase), and B. thuringiensis (Bth-RNase). These protein structures have not been experimentally determined. Although the cytotoxic action of above-mentioned ribonucleases is not yet proved, their close homology to barnase and binase suggests that these proteins should be tested as an antitumor drugs. The aim of this study is to determine the physicochemical properties of toxic ribonucleases and their close homologs. Few important characteristics, which are necessary for the unrevealing of the mechanism of ribonuclease cytotoxicity, namely charge, dipole moment, water-to-bilayer transfer free energy, and hydrophobic moment values were calculated. The molecular electrostatic maps of toxic ribonucleases were also obtained. The peculiarity of this investigation consists in the complex view on the lipid-protein interaction, which includes not only the electrostatical component, but also the hydrophobic component.

IBCH: 6821
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