muramidase and catechol

The interaction of metallodrugs with proteins influences their transport, uptake, and mechanism of action. In this study, we present an integrative approach based on spectroscopic (EPR) and computational (docking) tools to elucidate the noncovalent binding modes of various V

Topics: Binding Sites; Catechols; Coordination Complexes; Electron Spin Resonance Spectroscopy; Flavonoids; Hydrogen Bonding; Ligands; Molecular Docking Simulation; Muramidase; Pentanones; Protein Binding; Vanadium

Numerous phenolic compounds have been reported to have an inhibitory role on amyloid formation of proteins. The present study, utilizing lysozyme as a model system, examined the anti-amyloidogenic effects of phenol and three diphenol epimers. The results indicated that catechol and hydroquinone dose-dependently inhibited lysozyme fibrillation and covalently bound to the peptide chains to form quinoproteins, showing a similar effect to benzoquinone. In contrast, phenol and resorcinol did not modify the peptide with a quinone moiety, showing no effect on lysozyme fibrillation. We suggest that quinone intermediates are the active form for a phenolic compound to inhibit lysozyme fibrillation. The modification of lysozyme with quinone moieties alters the interacting forces between peptide chains and consequently interrupts the process of lysozyme fibrillation.

Topics: Amyloid; Benzoquinones; Catechols; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Hydroquinones; Kinetics; Microscopy, Electron, Transmission; Molecular Structure; Muramidase; Phenols; Protein Binding; Resorcinols