The inhibitory role of clioquinol in the fibrillation of hen egg white lysozyme

Here, we reported the role of clioquinol in amyloid aggregation of hen egg white lysozyme (HEWL) under stressful conditions by several biophysical methods including thioflavin-T (ThT) fluorescence, Congo red (CR), circular dichroism (CD) and transmission electron microscopy. Our work showed that CQ inhibited the fibril formation of HEWL and the inhibitory effects depended on the concentrations of CQ. Furthermore, fluorescence spectra were used to study the conformation changes of HEWL caused by CQ. These data revealed that the interactions of CQ with HEWL changed the tertiary structure and inhibited the hydrophobic exposure of HEWL.

Automated summary

The study demonstrated that clioquinol inhibits fibril formation of HEWL, with the inhibitory effects depending on the concentration of clioquinol. Fluorescence spectra showed that clioquinol induced conformational changes in HEWL, altering its tertiary structure and inhibiting hydrophobic exposure.