Amyloid fibrillogenesis of lysozyme is suppressed by a food additive brilliant blue FCF
Yu-Han Chen, Chia-Ping Tseng, Su-Chun How, Chun-Hsien Lo, Wei-Lung Chou, Steven S.-S. Wang
Colloids and Surfaces B: Biointerfaces
At least 30 different human proteins can fold abnormally to form the amyloid deposits that are associated with a number of degenerative diseases. The research presented here aimed at understanding the inhibitory potency of a food additive, brilliant blue FCF (BBF), on the amyloid fibril formation of lysozyme. Our results demonstrated that BBF was able to suppress the formation of lysozyme fibrils in a dose-dependent fashion. In addition, the structural features and conformational changes in the lysozyme samples upon the addition of BBF were further characterized using circular dichroism spectroscopy, nile red fluorescence spectroscopy, turbidity assay, and sodium dodecyl sulfate electrophoresis. Through molecular docking and molecular dynamics simulations, BBF’s mechanism of action in lysozyme fibrillogenesis inhibition was found to be initiated by binding with the aggregation-prone region of the lysozyme. We believe the results from this research may contribute to the development of effective therapeutics for amyloidoses.
Circular dichroism, Aggregation, Secondary structure, Biochemistry