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Citation: LIU Yong-Ming, LI Gui-Zhi, SONG Wan-Kun, WANG Jin-Jun. Molecular Simulation and Interaction between Human Serum Albumin and Topotecan Hydrochloride[J]. Acta Physico-Chimica Sinica, ;2006, 22(12): 1456-1459. doi: 10.3866/PKU.WHXB20061205 shu

Molecular Simulation and Interaction between Human Serum Albumin and Topotecan Hydrochloride

1.
(College of Chemistry, Yantai University, Yantai 264005, P. R. China)

Received Date: 8 May 2006
Available Online: 6 December 2006

The binding reaction between topotecan hydrochloride (THC) and human serum albumin (HSA) was studied by fluorescence and UV-Vis absorption spectra. The binding equilibrium constant, number of binding site and thermodynamic parameters were calculated. The distance between the binding site and tryptophan residue is 3.63 nm. The study of molecular simulation indicated that topotecan hydrochloride bound within the subdomain IIA of human serum albumins and the interaction between topotecan hydrochloride and HSA was dominated by hydrophobic force. In addition, both the residues Ala-291 and Asp-256 of HSA formed hydrogen bonds with topotecan hydrochloride, respectively.
- THC;HAS;Fluorescence quenching;Binding reaction;Molecular simulation
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