Study on interaction between tolbutamide and lactalbumin by spectroscopy and molecular docking
Objective To study the interaction between tolbutamide and lactalbumin under physiological conditions via fluorescence spectroscopy,ultraviolet spectroscopy and molecular docking.Methods The excitation wavelength of 280 nm was selected to measure the fluorescence quenching spectra at different temperatures.The quenching mechanism,the interaction characteristics between drug and lactalbumin,and the changes in the conformation of lactalbumin were determined by calculating related parameters(binding constant,number of binding sites,etc.)and thermodynamic parameters.The possible forms of interaction between drug and lactalbumin were explored by molecular docking method.Results Tolbutamide can cause lactalbumin endogenous fluorescence to occur by quenching by composite static quenching;the main force types are hydrogen bond and van der Waals force;It was inferred that non-radiative energy transfer occurred during the binding of tolbutamide to lactalbumin,which promoted the quenching of lactalbumin.Synchronous fluorescence spectroscopy,ultraviolet absorption spectroscopy and three-dimensional fluorescence spectra showed that the binding reaction had no obvious effect on the conformation of lactalbumin.The molecular docking results showed that tolbutamide formed one hydrogen bond with Glu113 residue,two hydrogen bonds with Asp116 residue and two hydrogen bonds with Glu121 residue.Conclusion Tolbutamide can spontaneously interact with lactalbumin.It is suggested that tolbutamide should not be taken with milk.
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