Interaction between alogliptin,linagliptin and lactalbumin by spectroscopy plus molecular docking
OBJECTIVE To examine the interaction between alogliptin,linagliptin and lactalbumin through fluorescent spec-troscopy,ultraviolet spectroscopy and molecular docking under physiological conditions.METHODS The excitation wave-length(λex)of 280 nm was selected for measuring the fluorescent quenching spectra at different temperatures.Quenching mecha-nism,interaction characteristics between drugs and lactalbumin and conformation changes of lactalbumin were determined by calcu-lating the related parameters(binding constant & number of binding sites)and thermodynamic parameters.The possible forms of interaction between drugs and lactalbumin were explored by molecular docking.RESULTS Both alogliptin and ligliptin could cause compound static quenching of lactalbumin.Hydrophobic force was a major force.According to ultraviolet absorption spec-trum,synchronous fluorescent spectrum and three-dimensional fluorescent spectrum,drug binding reaction had no obvious effect on the conformation of lactalbumin.Alogliptin and ligliptin formed hydrogen bonds with amino acid residues.CONCLUSION Alogliptin and ligliptin can spontaneously interact with lactalbumin.It is recommended not to take two drugs with milk.
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