Study of the interaction of deoxynivalenol with human serum albumin by spectroscopic technique and molecular modelling

• Published in: Food additives & contaminants. Part A, Chemistry, analysis, control, exposure & risk assessment Vol. 30; no. 2; pp. 356 - 364
• Main Authors: Li, Yuqin, Wang, Hao, Jia, Baoxiu, Liu, Caihong, Liu, Ke, Qi, Yongxiu, Hu, Zhide
• Format: Journal Article
• Language: English
• Published: Abingdon Taylor & Francis Group 01.02.2013; Taylor & Francis; Taylor & Francis Ltd
• Subjects: Binding Sites; Biological and medical sciences; Cadmium; Circular Dichroism; deoxynivalenol; Energy Transfer; Fluorescence; Fluorescence Resonance Energy Transfer; Food additives; Food contamination & poisoning; Food industries; Food toxicology; Fourier transforms; Fundamental and applied biological sciences. Psychology; human serum albumin; Humans; Hydrogen Bonding; Hydrogen bonds; Hydrophobic and Hydrophilic Interactions; hydrophobicity; interaction; Models, Molecular; molecular modelling; Molecules; Protein Conformation; protein secondary structure; Proteins; Risk assessment; Serum Albumin - chemistry; Serum Albumin - drug effects; Spectrometry, Fluorescence; spectroscopic technique; Spectroscopy; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Thermodynamics; Toxicology; Trichothecenes - chemistry; Trichothecenes - toxicity; Human; Toxin; deoxynivalenol; Interaction; molecular modelling; Mycotoxin; Vomitoxin; Serum albumin; human serum albumin; spectroscopic technique
• DOI: 10.1080/19440049.2012.742573
• ISSN: 1944-0057; 1944-0049

The mechanism of interaction between deoxynivalenol (DON) and human serum albumin (HSA) was studied using spectroscopic methods including fluorescence spectra, UV-VIS, Fourier transform infrared (FT-IR) and circular dichroism (CD). The quenching mechanism was investigated in terms of the association constants, number of binding sites and basic thermodynamic parameters. The distance between the HSA donor and the acceptor DON was 2.80 nm as derived from fluorescence resonance energy transfer. The secondary structure compositions of free HSA and its DON complexes were estimated by the FT-IR spectra. Alteration of the secondary protein structure in the presence of DON was confirmed by UV-VIS and CD spectroscopy. Molecular modelling revealed that a DON–protein complex was stabilised by hydrophobic forces and hydrogen bonding. It was potentially useful for elucidating the toxigenicity of DON when combined with biomolecular function effect, transmembrane transport, toxicological testing and the other experiments.