Spectroscopy and Spectral Analysis, Volume. 36, Issue 9, 3053(2016)
Research on Molecular Spectra of Interactions Between Salvianolic Acid A and Salvianolic Acid B with Insulin, and Effect of Glucose on the Binding
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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YANG Wen-yue, CUI Lin, QU Ling-ling, XU Ning, HUANG Yun, CUI Li-jian, ZHAN Wen-hong, ZHAO Ding. Research on Molecular Spectra of Interactions Between Salvianolic Acid A and Salvianolic Acid B with Insulin, and Effect of Glucose on the Binding[J]. Spectroscopy and Spectral Analysis, 2016, 36(9): 3053
Received: May. 6, 2015
Accepted: --
Published Online: Dec. 26, 2016
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