Theinteraction of patulin with human serum albumin (HSA) was studied in vitro under normal physiological conditions.The study\nwas performed using fluorescence, ultraviolet-visible spectroscopy (UV-Vis), circular dichroism (CD), atomic force microscopy\n(AFM), and molecular modeling techniques. The quenching mechanism was investigated using the association constants, the\nnumber of binding sites, and basic thermodynamic parameters. A dynamic quenching mechanism occurred between HSA and\npatulin, and the binding constants (K) were 2.60 Ã?â?? 104, 4.59 Ã?â?? 104, and 7.01 Ã?â?? 104M?1 at 288, 300, and 310 K, respectively. Based\non fluorescence resonance energy transfer, the distance between the HSA and patulin was determined to be 2.847 nm. The ?G0,\n?H0, and ?S0 values across various temperatures indicated that hydrophobic interaction was the predominant binding force. The\nUV-Vis and CD results confirmed that the secondary structure of HSA was altered in the presence of patulin. The AFM results\nrevealed that the individual HSA molecule dimensions were larger after interaction with patulin. In addition, molecular modeling\nshowed that the patulin-HSA complex was stabilized by hydrophobic and hydrogen bond forces. The study results suggested that a\nweak intermolecular interaction occurred between patulin and HSA. Overall, the results are potentially useful for elucidating the\ntoxigenicity of patulin when it is combined with the biomolecular function effect, transmembrane transport, toxicological, testing\nand other experiments.
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