Elucidating the molecular interaction of sinigrin, a potent anticancer glucosinolate from cruciferous vegetables with bovine serum albumin: effect of methylglyoxal modification

The present study employed the spectroscopic techniques, i.e. fluorescence, and circular dichroism (CD) and the molecular docking approach to investigate the mechanism of interaction of a potent anticancer glucosinolate, sinigrin (SIN), with bovine serum albumin (BSA). SIN binding to BSA resulted in the quenching of intrinsic fluorescence, and the analysis of results revealed the presence of static quenching mechanism. Based on the results, it was evident that the interaction of SIN with BSA was mainly stabilized by hydrogen bonding. Results from CD analysis revealed that the binding of SIN does not induce significant conformational changes in BSA. Molecular docking studies showed that four hydrogen bonds stabilize the binding of SIN in the site I of BSA with a binding energy of −6.2 kcal mol−1. These findings will not only provide insights about the mechanism of interaction of sinigrin but also showed the effect of methylglyoxal-mediated glycation on ligand binding with BSA.