Abstract
The interactions between the fungicide tebuconazole and human serum albumin were investigated using fluorescence and circular dichroism spectroscopies. The experimental results showed that the fluorescence quenching of the protein by the tebuconazole molecule was a result of the formation of a ligand-protein complex with a binding constant of 8.51×103 l.mol−1 and the number of binding sites in the macromolecule was close to 1. These findings demonstrated the fact that although the binding affinity of tebuconazole to the protein may be slight, it was very similar to other triazole fungicides. In addition, tebuconazole stabilized the α-helical secondary structure of the human serum albumin due to the increase of the α-content in the protein macromolecule.