مشخصات پژوهش

Aloin is a major glycosyl anthraquinone found in Aloe vera and exists as A and B diastomers. Based on previous studies, Aloin has pharmacological effects like anti-oxidation, anti-inflammation, and anti-tumor properties. Aloin is a light sensitive component and can be degraded to other derivatives like aloe-emodin, which has apoptotic induction properties. Aloin is able to enter blood flow quickly and reach body organs. So the study of Aloin interaction with proteins helps us with molecular information. In this study, we examined the interaction of Aloin and its’ derivatives with hen egg white lysozyme (HEWL). Lysozyme is an enzyme with anti-bacterial properties and is mostly found in all body fluids. It is used as a suitable model protein in molecular level detections. Unlike wide range cellular studies, no molecular level studies have been yet reported on the HEWL-Aloin interaction. We applied UV-vis and fluorescence spectroscopes in this study. In order to investigate the effects of Aloin and its’ derivatives, different concentrations of these ligands were added to HEWL (0.3 mg/ml) and its’ intrinsic absorbance and fluorescence were measured. Results showed absorbance intensity increase and fluorescence emission decrease of HEWL with increasing ligands concentration. Fluorescence quenching measurements were performed at different temperatures to find out the interaction mechanism. According to obtained Stern-Volmer constant, Aloin and its’ derivatives bind to HEWL by a dynamic and static mechanism, respectively. The results indicated also conformational changes of HEWL. Therefore, Aloin or its’ derivatives may be used as a drug by caution. However, further studies are needed to ensure Alion and its’ derivatives effects on the conformation of biological macromolecules.