Investigating the effects of erythrosine B on amyloid fibril formation derived from lysozyme

Chun Tien Kuo, Yi Lin Chen, Wei Tse Hsu, Su Chun How, Yu Hong Cheng, Shu Shun Hsueh, Hwai Shen Liu, Ta Hsien Lin, Josephine W. Wu, Steven S.S. Wang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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.

Original languageEnglish
Pages (from-to)159-168
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume98
DOIs
StatePublished - 1 May 2017

Keywords

  • Amyloid fibrils
  • Erythrosine B
  • Inhibition

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