Brilliant blue R dye is capable of suppressing amyloid fibril formation of lysozyme
Autor: | Steven S.-S. Wang, Su-Chun How, Chun-Hsien Lo, Wei-Tse Hsu, Chia-Ping Tseng, Wei-Lung Chou |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Amyloid Molecular Dynamics Simulation Protein Structure Secondary Protein Aggregates 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Structural Biology mental disorders Humans Molecular Biology Binding Sites Benzenesulfonates Fibrillogenesis General Medicine Amyloid fibril Molecular Docking Simulation 030104 developmental biology Biochemistry chemistry Muramidase Lysozyme 030217 neurology & neurosurgery Protein Binding |
Zdroj: | Journal of Biomolecular Structure and Dynamics. 36:3420-3433 |
ISSN: | 1538-0254 0739-1102 |
DOI: | 10.1080/07391102.2017.1388848 |
Popis: | Amyloid fibril formation is associated with an array of degenerative diseases. While no real cure is currently available, evidence suggests that suppression of amyloid fibrillogenesis is an effective strategy toward combating these diseases. Brilliant blue R (BBR), a disulfonated triphenylmethane compound, has been shown to interact with fibril-forming proteins but exert different effects on amyloid fibrillogenesis. These inconsistent findings prompted us to further evaluate BBR’s effect on the inhibition/suppresion of protein fibrillogenesis. Using 129-residue hen lysozyme, which shares high sequence homology to human lysozyme associated with hereditary non-neuropathic systemic amyloidosis, as a model, this study is aimed at thoroughly examining the influence of BBR on the in vitro protein fibrillogenesis. We first showed that BBR dose-dependently attenuated lysozyme fibril formation probably by affecting the fibril growth rate, with the value of IC50 determined to be ~4.39 μM. Next, we employed tryptophan fluorescence quenching method to determine the binding constant and number of binding site(s) associated with BBR-lysozyme binding. In addition, we further conducted molecular docking studies to gain a better understanding of the possible binding site(s) and interaction(s) between lysozyme and BBR. We believe some of the information and/or knowledge concerning the structure–function relationship associated with BBR’s suppressing activity obtained here can be applied for the future work in the subject matter related with the therapeutic strategies for amyloid diseases. |
Databáze: | OpenAIRE |
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