Investigation on the binding behaviors of two dihydrochalcones to bovine serum albumin and their anti-glycation activities

Abstract

The interactions of two dihydrochalcones (naringin dihydrochalcone (NGDC) and neohesperidin dihydrochalcone (NHDC)) with bovine serum albumin (BSA) and their anti-glycation effects were studied utilizing multiple spectral methods and molecular simulation technique. The findings proved that NGDC/NHDC could use a static quenching mechanism to reduce the intrinsic fluorescence of BSA, and the interaction between NGDC/NHDC and BSA was a spontaneous behavior with the binding constant ranging from 104 to 105M−1. Furthermore, NGDC and NHDC mainly interacted with the site I (subdomain IIA) of BSA via hydrophobic interactions and hydrogen bonds, endorsed by molecular docking study. A conjoint analysis of circular dichroism, three-dimensional fluorescence, dynamic light scattering, and UV-vis absorption spectra confirmed that NGDC/NHDC could induce some alterations in the spatial conformation and microenvironment of BSA. Additionally, NGDC and NHDC inhibited the non-enzymatic glycation of BSA by decreasing the contents of advanced glycation end products (AGEs), trapping methylglyoxal/glyoxal and maintaining the stability of the natural conformation of the protein. Overall, these findings were highly beneficial in disclosing the interaction mechanisms between dihydrochalcones and BSA and providing valuable information for the application of dihydrochalcones as functional food ingredients.