کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1405658 | 1501793 | 2012 | 6 صفحه PDF | دانلود رایگان |

In this report, the binding interaction of BPA with pepsin has been explored by spectroscopic and molecular modeling methods. Quenching of fluorescence of pepsin with increasing BPA concentration is a useful tool in the analysis of thermodynamic parameters. The results showed that the hydrophobic, steric contacts and hydrogen bonds interactions played major roles in stabilizing the complex. The binding of BPA to pepsin induced some micro-environmental and conformational changes in pepsin. The docking studies results showed that BPA entered into the hydrophobic cavity of pepsin. The interaction of pepsin with BPA occurs in the area between domain I and domain III.
► The interaction between BPA and pepsin is investigated by spectral and docking studies.
► The hydrophobic, steric contacts and hydrogen bonds interactions stabilize the BPA–pepsin complex.
► The interaction of pepsin with BPA occurs in the area between domain I and domain III.
► The three-dimensional fluorescence spectra of BPA–pepsin system is showed in paper.
Journal: Journal of Molecular Structure - Volume 1021, 15 August 2012, Pages 34–39