Molecular insight into the antiglycating and antiaggregating potential of ferulic acid with BSA

Abstract

Ferulic acid (FA) is one of the cinnamic acid derivatives and abundantly available in most cereals, fruits (orange), and vegetables (tomato, carrot). It has been characterized for its therapeutic potential against several diseases and disorders such as diabetes and Alzheimer’s. It exhibits promising antioxidant, anti-inflammatory, anticancer, and antiallergic, and many more properties. In the present study, the FA has been investigated for therapeutic insights through interaction behavior with protein and calculating binding and thermodynamic parameters at marked temperatures. Circular dichroism was employed for analyzing the secondary structure of the protein. The non-enzymatic glycation process was checked with parameters such as fructosamine and carbonyl content, total advanced glycated end products (AGEs), and individual AGE content spectroscopically. The glycation-induced aggregates of amyloid β-structure were measured with thioflavin-T and visualized using SDS-PAGE. The results indicate that the FA-provided physiological binding constant, Kb equals 1.364 × 104 M−1 at 25 ° C with bovine serum albumin (BSA). The dynamic interaction was observed to be spontaneous with negative Gibb’s energy. The FA potentially suppressed the glycated product formation and protein aggregation. Therefore, these findings suggest that FA may be a useful therapeutic drug candidate for the antiglycation and antiaggregation processes. Graphical abstract: [Figure not available: see fulltext.].