Citreoviridin (CIT), amycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and\ndetrimental to human and animal health. In this study, the interaction of CIT with human serum albumin (HSA) is researched by\nsteady-state fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD) methods, and molecular modeling. The\nassociation constants, binding site numbers, and corresponding thermodynamic parameters are used to investigate the quenching\nmechanism. The alternations of HSA secondary structure in the presence of CIT are demonstrated with UV-Vis, synchronous\nfluorescence, and CD spectra. The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with\nhydrophobic and hydrogen bond force. Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via\nfluorescence resonance energy transfer method.
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