Thymoquinone (TQ) is a bioactive component of medicinal plant, Nigella sativa. It has been identified as promising anti-inflammatory and anti-analgesic properties. In the present study, the TQ has been investigated for physiological interaction as well as binding properties with serum albumin and their thermodynamic parameters at different temperatures. Glycation process was checked with the measurement of fructosamine content, carbonyl content and total advanced glycated end products. The aggregation of amyloid β-structure was measured with Thioflavin-T and the secondary structure of BSA was observed by circular dichroism (CD) in glycated and thermal treated samples. The results indicate that the TQ showed binding interaction (both static and dynamic) with BSA (Kb= 18.31 × 107 M-1 at 293 K) and suppression of glycated products. The glycation-induced and thermal aggregation were prevented and the secondary structure of BSA was maintained. Therefore, these findings suggest that TQ may be used for a therapeutic drug for antiglycation as well as anti-aggregation.Communicated by Ramaswamy H. Sarma.
Keywords: Aggregation; BSA; advanced glycation end-products; glycation; protein binding interaction; thymoquinone.