title: Investigating the effects of erythrosine B on amyloid fibril formation derived from lysozyme.
abstract: Formation of amyloid fibrils has been associated with at least 30 different protein aggregation diseases. The 129-residue polypeptide hen lysozyme, which is structurally homologous to human lysozyme, has been demonstrated to exhibit amyloid fibril-forming propensity in vitro. This study is aimed at exploring the influence of erythrosine B on the in vitro amyloid fibril formation of hen lysozyme at pH 2.0 and 55°C using ThT binding assay, transmission electron microscopy, far-UV circular dichroism absorption spectroscopy, 1-anilinonaphthalene-8-sulfonic acid fluorescence spectroscopy, and synchronous fluorescence study. We found that lysozyme fibrillogenesis was dose-dependently suppressed by erythrosine B. In addition, our far-UV CD and ANS fluorescence data showed that, as compared with the untreated lysozyme control, the α-to-ß transition and exposure of hydrophobic clusters in lysozyme were reduced upon treatment with erythrosine B. Moreover, it could be inferred that the binding of erythrosine B occurred in the vicinity of the tryptophan residues. Finally, molecular docking and molecular dynamics simulations were further employed to gain some insights into the possible binding site(s) and interactions between lysozyme and erythrosine B. We believe the results obtained here may contribute to the development of potential strategies/approaches for the suppression of amyloid fibrillogenesis, which is implicated in amyloid pathology.
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Chun-Tien
authors.initials: CT
authors.lastname: Kuo
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Yi-Lin
authors.initials: YL
authors.lastname: Chen
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Wei-Tse
authors.initials: WT
authors.lastname: Hsu
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: Yu-Hong
authors.initials: YH
authors.lastname: Cheng
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Shu-Shun
authors.initials: SS
authors.lastname: Hsueh
authors.affiliation: Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Hwai-Shen
authors.initials: HS
authors.lastname: Liu
authors.affiliation: Department of Medical Research and Education, Taipei Veterans General Hospital, Taipei 102, Taiwan; Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 102, Taiwan.
authors.forename: Ta-Hsien
authors.initials: TH
authors.lastname: Lin
authors.affiliation: Department of Optometry, Central Taiwan University of Science and Technology, Taichung 40601, Taiwan. Electronic address: 107658@ctust.edu.tw.
authors.forename: Josephine W
authors.initials: JW
authors.lastname: Wu
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 / Q000737:chemistry*; D000818:Animals; D004923:Erythrosine / Q000378:metabolism / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization / Q000187:drug effects*; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D000682:Amyloid; C421864:hen egg lysozyme; D009113:Muramidase; D004923:Erythrosine
keywords: Amyloid fibrils; Erythrosine B; Inhibition