Comparison and investigation of bovine hemoglobin binding to dihydroartemisinin and 9-hydroxy-dihydroartemisinin: spectroscopic characterization.

Mengsi Xiao, Lina Han, Lin Zhou, Yanhuai Zhou, Xiaoqin Huang, Xuefeng Ge, Shaohua Wei, Jiahong Zhou, Heming Wu, Jian Shen

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy 2014 May 05

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The UV-vis absorption, steady state/time resolved fluorescence spectroscopy and synchronous fluorescence, circular dichroism (CD) spectroscopy are used to investigate the interaction mechanisms of dihydroartemisinin (DHA) and 9-hydroxy-dihydroartemisinin (9-OH DHA), respectively. The UV-vis studies present that DHA and 9-OH DHA can disturb the structure of bovine hemoglobin (BHb). Steady state/time resolved and synchronous fluorescence spectroscopy reveal that the binding constant of DHA with BHb is bigger than 9-OH DHA. CD spectra indicate DHA and 9-OH DHA can change the conformation of BHb. The comparison results suggest that the binding of BHb with DHA is more stable and stronger than 9-OH DHA. Copyright © 2014 Elsevier B.V. All rights reserved.

Citation

Mengsi Xiao, Lina Han, Lin Zhou, Yanhuai Zhou, Xiaoqin Huang, Xuefeng Ge, Shaohua Wei, Jiahong Zhou, Heming Wu, Jian Shen. Comparison and investigation of bovine hemoglobin binding to dihydroartemisinin and 9-hydroxy-dihydroartemisinin: spectroscopic characterization. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 2014 May 05;125:120-5