In this article

the interaction between halloysite nanotube and lysozyme used as model protein was studied by spectroscopic method. The fluorescence of lysozyme was quenched upon addition of halloysite nanotubes and the quenching mechanism belonged to static quenching. Intensity increase of resonance light scattering may be caused by the increase of molecular size as a result of halloysite nanotube-lysozyme complex formation

which was consistent with the data of UV-vis absorption spectra and static quenching mechanism. Interaction site between halloysite nanotubes and lysozyme was around the tryptophan in lysozyme based on synchronous fluorescence spectra

where the secondary structure of lysozyme was changed. When the concentrations of halloysite nanotubes were 100 mg/mL and 200 mg/mL

the decreased α-helix structure content were 3.28% and 6.89%

respectively

calculated by the data of circular dichroism spectra.