Mechanistic insight into glycation inhibition of human serum albumin by vitamin B9: Multispectroscopic and molecular docking approach

Advanced glycation end products (AGEs) formation produces free radicals that play a role in diabetes mellitus; hence inhibition of glycation plays a part in minimizing diabetes-related complications. This study was intended to examine the AGES formation of HSA upon prolonged incubation of 28 days at 37 degrees C and further investigate the antiglycation potential of folic acid (FA). FA shows a significant binding affinity to the HSA with a binding constant (K) of 10(4) M-1. The evaluation of enthalpy change (Delta H-0) and entropy change (Delta S degrees) implied that the HSA-FA complex is stabilized primarily by hydrophobic interaction and hydrogen bonding. Molecular docking analysis depicted that FA binds with HSA in subdomain IIA (Sudlow's site I) with a binding energy of -7.0 kcal mol(-1). AGEs were characterized by free lysine and thiol groups, carbonyl content, and AGEs specific fluorescence. The presence of FA significantly decreased glycation from free lysine and carbonyl content estimation and AGES specific fluorescence. Multispectroscopic observations and molecular docking and examination of various biomarkers demonstrate the antiglycation activity of FA and its capacity to prevent disease progression in diabetes. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study revealed that folic acid showed significant effects in inhibiting glycation and reducing the formation of AGEs. The binding between folic acid and HSA is primarily stabilized by hydrophobic interaction and hydrogen bonding in the complex. Various experimental results confirmed the antiglycation activity of folic acid.