Investigation on the interaction behavior between bisphenol A and pepsin by spectral and docking studies

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.