Exploring the effects of methylene blue on amyloid fibrillogenesis of lysozyme
| Autor: | Josephine W. Wu, Su Chun How, Zuzana Bednarikova, Steven S.-S. Wang, Andrea Antosova, Ta Hsien Lin, Jinn Tsyy Lai, Zuzana Gazova, Yu-Hong Cheng, Chun Hsien Lo |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Amyloid Molecular Conformation 02 engineering and technology Molecular Dynamics Simulation Fibril Protein Aggregation Pathological Biochemistry Protein Aggregates Structure-Activity Relationship 03 medical and health sciences chemistry.chemical_compound Structural Biology Molecular Biology Spectrum Analysis Fibrillogenesis Amyloidosis General Medicine 021001 nanoscience & nanotechnology Fluorescence Small molecule In vitro Methylene Blue Molecular Docking Simulation 030104 developmental biology chemistry Biophysics Muramidase Lysozyme 0210 nano-technology Methylene blue Protein Binding |
| Zdroj: | International Journal of Biological Macromolecules. 119:1059-1067 |
| ISSN: | 0141-8130 |
| Popis: | The 129-residue lysozyme has been shown to form amyloid fibrils in vitro. While methylene blue (MB), a compound in the phenothiazinium family, has been shown to dissemble tau fibril formation, its anti-fibrillogenic effect has not been thoroughly characterized in other proteins/peptides. This study examines the effects of MB on the in vitro fibrillogenesis of lysozyme at pH 2.0 and 55 °C. Our results demonstrated that, upon 7-day incubation, the plateau ThT fluorescence of the sample was found to be ~8.69% or ~2.98% of the control when the molar ratio of lysozyme to MB was at 1:1.11 or 1:3.33, respectively, indicating that the inhibitory potency of MB against lysozyme fibrillogenesis is positively correlated with its concentration. We also found that MB is able to destabilize the preformed lysozyme fibrils. Moreover, molecular docking and molecular dynamics simulations results revealed that MB's mechanism of fibril formation inhibition may be triggered by binding with lysozyme's aggregation-prone region. Results reported here provide solid support for MB's effect on amyloid fibrillogenesis. We believe the additional insights gained herein may pave way to the discovery of other small molecules that may have similar action toward amyloid fibril formation and its associated diseases. |
| Databáze: | OpenAIRE |
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