Brilliant blue R dye is capable of suppressing amyloid fibril formation of lysozyme
Journal
Journal of Biomolecular Structure and Dynamics
Journal Volume
36
Journal Issue
13
Pages
3420-3433
Date Issued
2018
Author(s)
Abstract
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 IC 50 determined to be ~4.39?£gM. 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¡Vfunction 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. ? 2017, ? 2017 Informa UK Limited, trading as Taylor & Francis Group.
Subjects
amyloid fibril
brilliant blue
lysozyme
suppression
SDGs
Other Subjects
amyloid; brilliant blue; brilliant blue R; lysozyme; unclassified drug; amyloid; benzenesulfonic acid derivative; brilliant blue; hen egg lysozyme; lysozyme; protein aggregate; protein binding; Article; binding affinity; binding site; circular dichroism; concentration response; controlled study; Fourier transform infrared spectroscopy; hydrophobicity; IC50; molecular docking; polyacrylamide gel electrophoresis; priority journal; protein aggregation; protein secondary structure; sequence homology; spectrofluorometry; structure activity relation; biosynthesis; chemistry; human; molecular dynamics; physiology; Amyloid; Benzenesulfonates; Binding Sites; Humans; Molecular Docking Simulation; Molecular Dynamics Simulation; Muramidase; Protein Aggregates; Protein Binding; Protein Structure, Secondary
Type
journal article