Amyloid aggregation of lysozyme: The synergy study of red wine polyphenols

• DOI: 10.1002/prot.24250
• Publication Date: 2013-02-13T15:22:41Z
• Authors: Zuzana Gazova; Katarina Siposova; Elena Kurin; Pavel Mučaji; Milan Nagy
• Keywords: Depolymerization; Thioflavin; Amyloid (mycology)

Abstract The amyloidoses are diseases associated with nonnative folding of proteins and characterized by the presence protein amyloid aggregates. ability quercetin, resveratrol, caffeic acid, their equimolar mixtures to affect aggregation hen egg white lysozyme in vitro was detected Thioflavin T fluorescence assay. anti‐amyloid activities tested polyphenols were evaluated median depolymerization concentrations DC 50 inhibition IC . Single substances more efficient (by at least one order) aggregates assay than formation 10 −4 −5 M range. Analyzed mixture samples showed synergic or antagonistic effects both assays. values ranged from −8 −9 , respectively. We observed that certain studied can synergistically inhibit production amyloids also effective Synergic correlated protein–small ligand docking studies AFM results. Differences these could be explained binding each polyphenol a different amino acid sequence within protein. Our results indicate synergic/antagonistic depend on selective known amyloidogenic sequences chain. findings reduction utter physiological relevance considering bioavailability low toxicity phenols. Proteins 2013; © 2012 Wiley Periodicals, Inc.