Analysis of binding properties and interaction of thiabendazole and its metabolite with human serum albumin via multiple spectroscopic methods

Food Chemistry
Qiaomei SunHui Li

Abstract

Thiabendazole (TBZ), which is oxidized into 5-hydroxythiabendazole (5-OH-TBZ) in vivo, is a commonly used food preservative. Interactions of TBZ and 5-OH-TBZ with human serum albumin (HSA) were comprehensively studied via multiple spectroscopic methods and molecular docking. This study focussed on the mechanistic and structural information on binding of TBZ and 5-OH-TBZ to HSA to evaluate the impact of the food additive on HSA. (1)H NMR spectra of the two ligands showed the binding exists. ITC and fluorescence spectroscopy results revealed that TBZ was a stronger ligand, with a binding constant of 10(5)l/mol and formed a more stable complex with HSA than did 5-OH-TBZ via electrostatic interaction. Spectroscopic results (UV-vis, FT-IR, and CD) showed that TBZ and 5-OH-TBZ caused conformational changes in HSA, in which α-helix and β-turn transformed into β-sheet, causing HSA structure to loosen. Docking programs showed that both TBZ and 5-OH-TBZ bound to HSA via IB.

Citations

Jul 16, 2019·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Masoomeh ShaghaghiAzam Aghamohammadi
Jan 23, 2021·European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences·Yuanhao LiangYufeng Liu
Mar 6, 2021·Journal of Biomolecular Structure & Dynamics·Sara Asadi FarsadSomaieh Soltani
May 1, 2021·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Qiaomei SunHui Li
Jul 18, 2021·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·Xiaolan LvXun Tuo
Aug 7, 2021·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Yue XingHongliang Xu
Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ruichen ZhaoJinfeng Zhong

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