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Citation: CAO Tuan-Wu, ZHOU Kun, HUANG Wen-Bing, SHI Jian-Wei, TAN Xiao-Ping, HUANG Chun-Lin, RAN Ai. Spectroscopic Study of Interaction of Harpagoside and Human Serum Albumin[J]. Chinese Journal of Analytical Chemistry, ;2017, 45(5): 700-706. doi: 10.11895/j.issn.0253-3820.160873 shu

Spectroscopic Study of Interaction of Harpagoside and Human Serum Albumin

Laboratory of Natural Medicine Research and Development in Wuling Mountain, School of Chemistry and Chemical Engineering, Yangtze Normal University, Chongqing 408100, China

Received Date: 30 November 2016
Revised Date: 8 March 2017

Fund Project: This work was supported by the Science and Technology Project of Chongqing Municipal Education Commission (No.KJ15012010), and the Construction of Scientific Research Platform of Yangtze Normal University (No.2015XJPT01).

Harpagoside (HAR) is believed to be a main compound in Scrophularia ningpoensis which possess a broad of biological activities. Human serum albumin (HSA) has important physiological roles in transportation, distribution and metabolism of many endogenous and exogenous substances in body. It is great significance in pharmacology to investigate the interaction mechanism of HAR and HSA. In this work, the interaction between HAR and HSA was investigated by fluorescence and ultraviolet absorption spectroscopy at different pH (pH=4.0, 7.4, and 9.0) and temperatures (297, 310 and 323 K). The experimental results showed that the HAR could cause the fluorescence quenching of HSA through a static quenching procedure, showing that the HAR regularly quenched the intrinsic fluorescence of HSA, and a decrease in the quenching constant was observed with an increase in temperature. Under different conditions, all the magnitude of binding constants (K_A) was larger than 10⁵ L/mol and the number of binding sites (n) in the binary system were approximate to 1. Base on the magnitude of enthalpy and entropy changes, the negative values of ΔG, ΔH and ΔS revealed that the binding of HAR with HSA was spontaneous and exothermic process, and the main interaction forces of the HAR with HAR were van der Waals forces and/or hydrogen bonding interaction. The binding distance (r) between the HAR and HSA was calculated to be about 4.2 nm based on the theory of Frster's nonradiation energy transfer, which indicated that the energy transfer from HSA to HAR occurred with high possibility. What was more, the synchronous florescence spectroscopy confirmed the conformational changes of HSA during the binding reaction.
- Scrophularia ningpoensis,
- Harpagoside,
- Human serum albumin,
- Fluorescence quenching,
- Binding interaction
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