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  3. Examining the inhibitory potency of food additive fast green FCF against amyloid fibrillogenesis under acidic conditions

Examining the inhibitory potency of food additive fast green FCF against amyloid fibrillogenesis under acidic conditions

  • Food Funct. 2016 Dec 7;7(12):4898-4907. doi: 10.1039/c6fo00792a.
Su-Chun How 1,  Szu-Ming Yang 1,  Ai Hsin 1,  Chia-Ping Tseng 1,  Shu-Shun Hsueh 1,  Ming-Shen Lin 2,  Rita P-Y Chen 3,  Wei-Lung Chou 4,  Steven S-S Wang 1
Affiliations

Affiliations

  • 1 Department of Chemical Engineering, National Taiwan University, Taipei 10617, Taiwan. sswang@ntu.edu.tw.
  • 2 TA Instruments-Waters LLC Taipei, Taiwan.
  • 3 Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan and Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
  • 4 Department of Safety, Health and Environmental Engineering, Hungkuang University, Sha Lu, Taichung City 433, Taiwan. wlchou@sunrise.hk.edu.tw.
PMID: 27824368 DOI: 10.1039/c6fo00792a
Abstract

More than thirty human proteins and/or Peptides can fold incorrectly to form amyloid deposits associated with several protein aggregation diseases. No cure is currently available for treating these diseases. This work is aimed at examining the inhibitory potency of fast green FCF, a biocompatible dye, toward the fibrillogenesis/aggregation of lysozyme. As verified by ThT binding assay along with transmission electron microscopy, fast green FCF was observed to suppress the generation of lysozyme fibrils in a concentration-dependent manner. We next used circular dichroism absorption spectroscopy, ANS fluorescence spectroscopy, and SDS-PAGE to characterize the structural alterations in lysozyme samples upon the addition of fast green FCF. Furthermore, experiments with the addition of fast green FCF at different time points of incubation showed that fast green FCF also exhibited disaggregating activity against the preformed/existing lysozyme fibrils. We believe that the results from this study suggest a potential therapeutic role of biocompatible molecules in treating or preventing protein aggregation diseases.

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