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Molecular transport mechanism of pefloxacin mesylate binding with transferrin / 药学学报
Acta Pharmaceutica Sinica ; (12): 1503-10, 2012.
Article in Chinese | WPRIM | ID: wpr-433005
ABSTRACT
The binding mechanism between pefloxacin mesylate (PM) and transferrin (Tf) was explored using spectral experiment combined with molecular modeling techniques. The binding parameters and thermodynamic functions of PM-Tf solution system were measured at different temperatures. The effect of PM on molecular conformation of Tf was investigated and the interaction mechanism was also discussed. The results showed that dynamic quenching mechanism occurs with PM binding to Tf. The value of binding distances (r) is low, which indicates the occurrence of energy transfer. The drug had conformational effect on Tf, which resulted in changes of hydrophobic environment of the binding domain in Tf. According to the obtained thermodynamic parameters, the main interaction force between PM and Tf is attributed to hydrophobic bonding. The results of molecular modeling revealed that hydrophobic and hydrogen bonds are main binding forces in the PM-Tf system. These results were in accordance with spectral experiments. The research results have given a better theoretical reference for the study of pharmacological mechanism between protein and quinolone.
Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Acta Pharmaceutica Sinica Year: 2012 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Language: Chinese Journal: Acta Pharmaceutica Sinica Year: 2012 Type: Article