The aim of this work was to evaluate interaction between aflatoxin M1 (AFM1) and structural models of β-lactoglobulin (β-LG) at pH 4.0 and 6.5. This information would provide an explanation of the variability in AFM1 during cheese production. Once β-LG models were optimized using molecular dynamic (MD) simulation, it was found that a region of the Calyx cavity underwent conformational changes, at the E-F loop, from the closed conformation at pH 6.5 to the open at pH 4.0. No differences in Site C conformation were observed at both pH. The binding free energy (ΔGb) of the β-LG-AFM1 complexes at the different pHs were determined by molecular docking. The ΔGb values obtained for the Calyx cavity showed that at pH 4.0 there is a more stable complex formation compared to pH 6.5 with values of -42.6 and -32.0 kJ mol-1, respectively. On the contrary, in the complexes formed in Site C at both pH´s there were no differences. Likewise, the ΔGb in the dimer interface was evaluated, obtaining a value of -29.3 kJ mol-1, like those obtained at Site C. In addition, by the MD simulations of the β-LG-AFM1 complexes, it was observed that at acidic pH the binding of AFM1 with β-LG is more stable. In conclusion, the computational tools showed that the most stable complex was formed at the Calyx cavity at pH 4.0. This suggests that during cheese production using acidic coagulation, the whey proteins show higher affinity toward AFM1 which may explain the observed variability of mycotoxin.Communicated by Ramaswamy H. Sarma.
Keywords: Molecular docking; Tanford transition; aflatoxin M1; molecular dynamics simulations; β-lactoglobulin.