Interaction of cadmium telluride semiconductor nanoparticles on egg white lysozyme using spectroscopic methods and enzymatic kinetics

In this article, the interaction between lysozyme and CdTe nanoparticles was investigated by UV-Vis spectroscopy, fluorescence, thermal stability, kinetics, and circular dichroism (CD) spectroscopic methods at pH 7.25. It was proved that the fluorescence quenching of lysozyme by CdTe NPs was mainly a result of the formation of the CdTe–lysozyme complex. By the fluorescence quenching results, the Stern–Volmer quenching constant (KSV), binding constant (Ka), and binding sites (n) were calculated. Under pH 7.25 conditions, the level of binding constant is determined to be 2.33×103 from fluorescence data. The hydrogen bond or van der Waals force is involved in the binding process. The blue shift of the fluorescence spectral peak of protein after the addition of CdTe nanoparticles reveals that the microenvironments around tryptophan residues are disturbed by CdTe nanoparticles. The effect of CdTe NPs on the conformation of lysozyme has been analyzed by means of UV-Vis spectra and CD spectra, which provided evidence that the secondary structure of lysozyme has been changed by the interaction of CdTe NPs with lysozyme.