Research on Molecular Spectra of Interactions Between Salvianolic Acid A and Salvianolic Acid B with Insulin, and Effect of Glucose on the Binding

• Published in: Guang pu xue yu guang pu fen xi Vol. 36; no. 9; p. 3053
• Main Authors: Yang, Wen-yue, Cui, Lin, Qu, Ling-ling, Xu, Ning, Huang, Yun, Cui, Li-jian, Zhan, Wen-hong, Zhao, Ding
• Format: Journal Article
• Language: English
• Published: China 01.09.2016
• ISSN: 1000-0593
• DOI: 10.3964/j.issn.1000-0593(2016)09-3053-09

The interactions of Salvianolic acis 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-belices and β-sheets no clear change. The glucose might influenced 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-belices.