Studies on the interaction of salvianolic acid B with human hemoglobin by multi-spectroscopic techniques |
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Authors: | Chen Tingting Zhu Shajun Cao Hui Shang Yanfang Wang Miao Jiang Guoqing Shi Yujun Lu Tianhong |
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Institution: | School of Chemistry and Chemical Engineering, Nantong University, Nantong, PR China. |
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Abstract: | The interaction between salvianolic acid B (Sal B) and human hemoglobin (HHb) under physiological conditions was investigated by UV-vis absorption, fluorescence, synchronous fluorescence and circular dichroism spectroscopic techniques. The experimental results indicate that the quenching mechanism of fluorescence of HHb by Sal B is a static quenching procedure, the binding reaction is spontaneous, and the hydrophobic interactions play a major role in binding of Sal B to HHb. Based on F?rster's theory of non-radiative energy transfer, the binding distance between Sal B and the inner tryptophan residues of HHb was determined to be 2.64 nm. The synchronous fluorescence experiment revealed that Sal B can not lead to the microenvironmental changes around the Tyr and Trp residues of HHb, and the binding site of Sal B on HHb is located at α(1)β(2) interface of HHb. Furthermore, the CD spectroscopy indicated the secondary structure of HHb is not changed in the presence of Sal B. |
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