Abstract
Over-accumulation of 3-Sulfanilamido-5-methylisoxazole (SMZ) and 2-sulfanilamido-4-methylpyrimidine (SMD) by organisms could lead to irreversible potential toxicity. Herein, the interaction mechanism of SMZ/SMD was demonstrated in combination with multispectral techniques, density functional theory (DFT) and molecular docking with the use of lysozyme (Lys) as a model protein. The quenching of Lys intrinsic fluorescence by SMD is greater than that by SMZ because the affinity of SMD for Lys is stronger than that of SMZ. The binding of SMD/SMZ to Lys is an exothermal process that is carried out automatically (ΔG<0), which is proved by thermodynamic parameters. The concept that the interaction between SMD/SMZ and Lys was mainly achieved through hydrogen bonding and hydrophobic interactions was also validated for molecular docking. These results reveal potential toxicological mechanisms about the interaction of SMD/SMZ with Lys and provide theoretical support for reducing the harm of sulfonamide antibiotics.
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