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邹国林, Kai Tang, Yi-Min Qin, Ai-Hua Lin, Xing Hu, Guo-Lin Zou*
Journal of Pharmaceutical and Biomedical Analysis 39 (2005) 404-410,-0001,():
-1年11月30日
Daunomycin (DM) is a clinically used antitumor anthracycline antibiotic, which is transported primarily by human serum albumin (HSA) in the blood. Binding characteristics are therefore of interest for both the pharmacokinetics and pharmacodynamics of DM. A new optical biosensor technique based on the resonant mirrorwas used to characterize interaction ofDMwith HSA at different temperatures and the affinity constants were obtained. The HSA-DM interaction is exothermic with having favorable enthalpy and entropy followed by the integrated van't Hoff equation analysis. Fluorescence studies showed that DM has an ability to quench the intrinsic fluorescence of HSA through a static quenching procedure according to the Stern–Volmer equation and DM displays a pH-dependent binding affinity to HSA. Molecular modeling calculations showed that the DM binds HSA to a non-classical drug binding site and further analysis of the binding site of DM within the HSA molecule suggested that hydrophobic contacts, hydrogen bond formation and electrostatic interactions account for the binding of DM.
Human serum albumin, Daunomycin, Resonant mirror biosensor, IAsys, Binding thermodynamics, Fluorescence quenching
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【期刊论文】Chemical composition and antimicrobial activity of the essential oils of Chrysanthemum indicum
邹国林
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-1年11月30日
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邹国林
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邹国林
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