Lochnericine (LOC) is a component of Voacanga africana, which is a type of traditional medical food in Africa widely used for treating diseases. In this article, the interaction between LOC and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. Furthermore, Fourier transform infrared (FTIR), Raman and circular dichroism (CD) were used to investigate the structural changes of BSA. The experimental results consistently indicated that LOC changed the secondary structure of BSA. Three structure-similar components were used to study the interference experiments. The molecular modeling results showed that LOC could bind within not only sites I and II, but also bind the cavity of subdomain IB.
Keywords: bovine serum albumin (BSA); interaction; lochnericine; molecular modeling; structural changes.
Copyright © 2014 John Wiley & Sons, Ltd.