| 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, China
3. 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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