The noncovalent conjugations of bovine serum albumin with three structurally different phytosterols exerted antiglycation effects: A study with AGEs-inhibition, multispectral, and docking investigations
Remah Sobhy, Fuchao Zhan, Enas Mekawi, Ibrahim Khalifa, Hongshan Liang, Bin Li
The antiglycation effects of three structurally different phytosterols (PS) including stigmasterol, β-sitosterol, and γ-oryzanol on bovine serum albumin (BSA) were deeply studied in a BSA-glucose model by measuring the glycoxidation-based products, SDS-PAGE intensity, free lysine, and their fluorescence microscopy clicks. For the first time, the underlying mechanisms of the antiglycation effects of PS were wholly elucidated by measuring their interaction ability with BSA and their antiradical activity during the glycation reactions. The results showed that PS could partially inhibit the formation of advance glycation end products, block some of the lysyl residues of BSA (Lys127, 357, 434, and 524), prevent the glucose-BAS bonding, and their disaggregation effects on the glycated BSA. Throughout the underlying mechanism behind the antiglycation activity, PS were found to structurally quench the fluorescence intensity of BSA in a static mode, leading to fluctuations in its Z-average size, UV–vis spectrum, and secondary structure. Additionally, PS mitigated the formation the advanced glycation end products by scavenging the radicals produced during the glycation reactions. Overall, these results unleash that PS prevent the glycation reactions and their subsequent changes through shielding the NH2 groups via H-bonding with their OH-groups and pi-pi interaction of the steroid core, besides the antiradical activity of PS on the free radicals generating during the glycation reactions.
Circular dichroism, Protein folding, Secondary structure, Chemical stability, Food science, Biochemistry