کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5746724 | 1618786 | 2017 | 7 صفحه PDF | دانلود رایگان |
- Interaction of pepsin with dicyandiamide were examined.
- Dicyandiamide binding affects the native structure of pepsin.
- Binding is moderate and dicyandiamide mainly binds at hydrophobic cavity of pepsin.
Dicyandiamide (DCD), considered to be a nitrification inhibitor, poses threat to human's health with exposure from milk, infant formula and other food products. In this work, DCD was investigated for its binding reaction with pepsin using spectroscopy and docking methods. Fluorescence experiments indicated DCD quenched the fluorescence of pepsin through a static process. Thermodynamic analysis of the binding data (ÎH0Â =Â â21.72Â kJÂ molâ1 and ÎS0Â =Â 17.61Â JÂ molâ1 Kâ1) suggested the involvement of hydrophobic and hydrogen bonding in the complex formation. The pepsin interacted with DCD at a hydrophobic cavity, leading to a conformational changes in the pepsin, as revealed from UV-vis absorption, Fourier transform infrared, the time-resolved fluorescence, three-dimensional fluorescence and circular dichroism spectral results.
Journal: Chemosphere - Volume 185, October 2017, Pages 1056-1062