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 |
ISSN: | 0065-2598 |
ISBN: | 978-3-319-18364-0 |
Publisher: | Springer |
Volume: | 863 |
Page Range: | 139-161 |
Date: | 2015 |
Additional Information: | Copyright © 2015 Springer International Publishing Switzerland |
Official Publication: | https://doi.org/10.1007/978-3-319-18365-7_7 |
External Fulltext: | View full text on PubMed Central |
PubMed: | View item in PubMed |
Repository Staff Only: item control page