title: Amyloid fibrillogenesis of lysozyme is suppressed by a food additive brilliant blue FCF.
abstract: 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.
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Yu-Han
authors.initials: YH
authors.lastname: Chen
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Chia-Ping
authors.initials: CP
authors.lastname: Tseng
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Su-Chun
authors.initials: SC
authors.lastname: How
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Chun-Hsien
authors.initials: CH
authors.lastname: Lo
authors.affiliation: Department of Safety, Health and Environmental Engineering, Hungkuang University, Sha Lu, Taichung City 433, Taiwan. Electronic address: wlchou@sunrise.hk.edu.tw.
authors.forename: Wei-Lung
authors.initials: WL
authors.lastname: Chou
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan. Electronic address: sswang@ntu.edu.tw.
authors.forename: Steven S-S
authors.initials: SS
authors.lastname: Wang
mesh_terms: D000682:Amyloid / Q000037:antagonists & inhibitors / Q000737:chemistry*; D000818:Animals; D001557:Benzenesulfonates / Q000737:chemistry*; D001665:Binding Sites; D002645:Chickens; D005503:Food Additives / Q000737:chemistry*; D007700:Kinetics; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000037:antagonists & inhibitors / Q000737:chemistry*; D066329:Protein Aggregates; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D001557:Benzenesulfonates; D005503:Food Additives; D066329:Protein Aggregates; D009113:Muramidase; C006796:brilliant blue
keywords: Aggregation; Amyloid fibrils; Brilliant blue FCF; Fibrillogenesis; Inhibition; Lysozyme