| 光谱学与光谱分析 |
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| Research on Molecular Spectra of Interactions Between Salvianolic Acid A and Salvianolic Acid B with Insulin, and Effect of Glucose on the Binding |
| YANG Wen-yue1, CUI Lin1, QU Ling-ling1, XU Ning1, HUANG Yun1,2*, CUI Li-jian3*, ZHAN Wen-hong1, ZHAO Ding1 |
| 1. Pharmaceutical College, Hebei Medical University, Shijiazhuang 050017, China 2. Institute of Chinese Integrative Medicine, Hebei Medical University, Shijiazhuang 050017, China3. Experimental Center, Hebei University of Chinese Medicine, Shijiazhuang 050091, China |
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Abstract The interactions of Salvianolic acid A (SAA) and Salvianolic acid B (SAB) with insulin were studied by using fluorescence spectroscopy, UV-vis spectroscopy and ATR-FTIR spectroscopy in simulating physiological condition (pH 7.40). The fluorescence quenching of insulin by SAA and SAB were static quenching process. The results of synchronous fluorescence and three-dimensional fluorescence spectra suggested no obvious conformation changes of insulin after SAA or SAB binding. But ATR-FTIR spectra showed that SAA and SAB could change the secondary structures of insulin, of which β-turns decreased and random coil increased accompanied with α-helices and β-sheets no clear change. The glucose might influenced the the bioactivity of insulin in the SAA-insulin and SAB-insulin systems by changing the binding constants of SAA (or SAB) with insulin and exacerbating the changes of insulin conformation and relative contents of α-helices.
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Received: 2015-05-06
Accepted: 2015-09-17
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Corresponding Authors:
HUANG Yun, CUI Li-jian
E-mail: huangyun9317@126.com; cuilijianzy@126.com
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