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

doi:10.1016/j.saa.2014.01.096

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

Spectrochim Acta A Mol Biomol Spectrosc. 2014 May 5:125:120-5. doi: 10.1016/j.saa.2014.01.096. Epub 2014 Jan 30.

Authors

Mengsi Xiao¹, Lina Han¹, Lin Zhou¹, Yanhuai Zhou², Xiaoqin Huang², Xuefeng Ge¹, Shaohua Wei¹, Jiahong Zhou³, Heming Wu⁴, Jian Shen¹

Affiliations

¹ Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, College of Chemistry and Materials Science, Analysis and Testing Center, Nanjing Normal University, Nanjing 210023, China; Jiangsu Key Laboratory of Biomedical Materials, College of Chemistry and Materials Science, Analysis and Testing Center, Key Laboratory of Applied Photochemistry, Nanjing Normal University, Nanjing 210023, China.
² Department of Physical Science and Technology, Nanjing Normal University, Nanjing 210023, China.
³ Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, College of Chemistry and Materials Science, Analysis and Testing Center, Nanjing Normal University, Nanjing 210023, China; Jiangsu Key Laboratory of Biomedical Materials, College of Chemistry and Materials Science, Analysis and Testing Center, Key Laboratory of Applied Photochemistry, Nanjing Normal University, Nanjing 210023, China. Electronic address: zhoujiahong@njnu.edu.cn.
⁴ Institute of Stomatology, Department of Oral and Maxillofacial Surgery, Nanjing Medical University, No. 136, Hanzhong Avenue, Nanjing, China. Electronic address: whmz2002@yahoo.cn.

PMID: 24531541
DOI: 10.1016/j.saa.2014.01.096

Abstract

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.

Keywords: 9-OH DHA; Bovine hemoglobin; Comparison; DHA; Spectroscopic characterization.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Artemisinins / chemistry*
Artemisinins / metabolism*
Cattle
Circular Dichroism
Hemoglobins / chemistry
Hemoglobins / metabolism*
Kinetics
Protein Binding
Protein Structure, Secondary
Solutions
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Thermodynamics
Time Factors

Substances

9-hydroxy-dihydroartemisinin
Artemisinins
Hemoglobins
Solutions
artenimol