Quinine (Qi) is a well-known drug used in malaria therapy; it is also a potential anti-arrhythmic drug used in the treatment of calf cramps, rheumatoid arthritis, colds, and photodermatitis. Moreover, it is used in the food industry for the production of tonics. This study aimed to analyze the interaction between quinine and a transporting protein-human serum albumin (HSA)-as well as the influence of Qi on both protein reduction and antioxidant potential. It was found that Qi (via spectrofluorometric measurements and circular dichroism spectroscopy) binds to HSA with a low affinity and slightly affects the secondary structure of albumin. As demonstrated by the use of ABTS and FRAP assays, HSA has a higher antioxidant and reduction potential than Qi, while their mutual interaction results in a synergistic effect in antioxidant activity and reduction potential.
Keywords: antioxidant and reduction potential; human serum albumin; quinine; spectroscopy.