مشخصات پژوهش

Introduction: Aloin that is known as a glycosyl anthraquinone, found in the leaves of Aloe Vera plant. As a natural compound possessing different pharmacological properties, Aloin has been considered for its possible drug potentials. It has been reported that aloin could induce apoptotic effect because of its anti-oxidation, anti-inflammation, and anti-tumor properties [1,2]. Because of the fast entrance of Aloin to the blood, it is possible to interact with different blood carrier proteins and reach the organs. Human serum albumin (HSA) is one of the most abundant proteins in the blood and responsible for drug transport [3]. Therefore, in this study we aimed to detect binding properties of Aloin with HSA by spectroscopic methods to find out more molecular information. Methods: In order to study the interaction, absorbance and fluorescence spectroscopies were applied. Different concentrations of Aloin and its light degradated derivatives were titrated to HSA solution with a final concentration of 5 µM. The experiments were done at different temperatures (25 to 37 ºC). Results and discussion: Based on UV-vis examinations, HSA absorbance intensity increased and fluorescence emission decreased gradually after drug addition. By use of quenching phenomena, binding data such as Stern-Volmer constant (Ksv), binding constant (Kb) and hill equation derived binding sites (n) were obtained. Results showed that Aloin and its derivatives bind non-spontaneously to HSA. The ligand formed a complex with HAS and bound to HSA through one binding site.Conclusion: It is concluded that the ligands are able to bind HSA and may induce some conformational alteration to it during transport to the target.