Chen Y.-H.Tseng C.-P.How S.-C.Lo C.-H.Chou W.-L.Wang S.S.-S.2019-05-092019-05-09201609277765https://scholars.lib.ntu.edu.tw/handle/123456789/406720At 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. ? 2016 Elsevier B.V.AggregationAmyloid fibrilsBrilliant blue FCFFibrillogenesisInhibitionLysozyme[SDGs]SDG3Agglomeration; Circular dichroism spectroscopy; Dichroism; Electrophoresis; Enzyme inhibition; Fluorescence spectroscopy; Food additives; Glycoproteins; Molecular dynamics; Proteins; Sodium dodecyl sulfate; Sodium sulfate; Amyloid fibril; Amyloid fibril formation; Brilliant blue FCF; Conformational change; Degenerative disease; Fibrillogenesis; Mechanism of action; Molecular dynamics simulations; Enzymes; amyloid; brilliant blue; food additive; lysozyme; amyloid; benzenesulfonic acid derivative; brilliant blue; food additive; lysozyme; protein aggregate; protein binding; amyloidosis; Article; assay; circular dichroism; controlled study; electrophoresis; enzyme activity; enzyme binding; fluorescence spectroscopy; molecular docking; molecular dynamics; molecular model; nile red fluorescence spectroscopy; pathogenesis; priority journal; protein aggregation; protein conformation; simulation; sodium dodecyl sulfate electrophoresis; turbidity assay; animal; antagonists and inhibitors; binding site; chemistry; chicken; kinetics; protein folding; protein secondary structure; Amyloid; Animals; Benzenesulfonates; Binding Sites; Chickens; Food Additives; Kinetics; Molecular Docking Simulation; Molecular Dynamics Simulation; Muramidase; Protein Aggregates; Protein Binding; Protein Folding; Protein Structure, Secondaryjournal article10.1016/j.colsurfb.2016.02.0642-s2.0-84960426259https://www.scopus.com/inward/record.uri?eid=2-s2.0-84960426259&doi=10.1016%2fj.colsurfb.2016.02.064&partnerID=40&md5=be249cdd36063c774f38d443c94c4394