Amyloid fibrillogenesis of lysozyme is suppressed by a food additive brilliant blue FCF
| Autor: | Steven S.-S. Wang, Wei-Lung Chou, Su-Chun How, Yu-Han Chen, Chia-Ping Tseng, Chun-Hsien Lo |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Protein Folding Circular dichroism 02 engineering and technology Molecular Dynamics Simulation Protein aggregation Fibril Protein Structure Secondary Protein Aggregates 03 medical and health sciences chemistry.chemical_compound Colloid and Surface Chemistry Animals Physical and Theoretical Chemistry Binding Sites Chemistry Benzenesulfonates Nile red Fibrillogenesis Surfaces and Interfaces General Medicine 021001 nanoscience & nanotechnology Molecular Docking Simulation Kinetics 030104 developmental biology Brilliant Blue FCF Biochemistry Food Additives Muramidase Protein folding Lysozyme 0210 nano-technology Chickens Protein Binding Biotechnology |
| Zdroj: | Colloids and Surfaces B: Biointerfaces. 142:351-359 |
| ISSN: | 0927-7765 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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