muramidase and resorcinol

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