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The effect of (-)-Epigallo-catechin-(3)-gallate on amyloidogenic proteins suggests a common mechanism

Item Type:Article
Title:The effect of (-)-Epigallo-catechin-(3)-gallate on amyloidogenic proteins suggests a common mechanism
Creators Name:Andrich, K. and Bieschke, J.
Abstract:Studies on the interaction of the green tea polyphenol (-)-Epigallocatechin-3-gallate (EGCG) with fourteen disease-related amyloid polypeptides and prions Huntingtin, Amyloid-beta, alpha-Synuclein, islet amyloid polypeptide (IAPP), Sup35, NM25 and NM4, tau, MSP2, semen-derived enhancer of virus infection (SEVI), immunoglobulin light chains, beta-microglobulin, prion protein (PrP) and Insulin, have yielded a variety of experimental observations. Here, we analyze whether these observations could be explained by a common mechanism and give a broad overview of the published experimental data on the actions of EGCG. Firstly, we look at the influence of EGCG on aggregate toxicity, morphology, seeding competence, stability and conformational changes. Secondly, we screened publications elucidating the biochemical mechanism of EGCG intervention, notably the effect of EGCG on aggregation kinetics, oligomeric aggregation intermediates, and its binding mode to polypeptides. We hypothesize that the experimental results may be reconciled in a common mechanism, in which EGCG binds to cross-beta sheet aggregation intermediates. The relative position of these species in the energy profile of the amyloid cascade would determine the net effect of EGCG on aggregation and disaggregation of amyloid fibrils.
Keywords:Epigallocathechin-3-gallate (EGCG), Amyloid Polypeptides, Aggregation, Fibrils, Animals
Source:Advances in Experimental Medicine and Biology
Series Name:Advances in Experimental Medicine and Biology
Title of Book:Natural compounds as therapeutic agents for amyloidogenic diseases
Page Range:139-161
Official Publication:https://doi.org/10.1007/978-3-319-18365-7_7
PubMed:View item in PubMed

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