Abstract Title:

Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity.

Abstract Source:

FEBS Lett. 2009 Nov 19;583(22):3569-76. Epub 2009 Oct 25. PMID: 19861125

Abstract Author(s):

Nelson Ferreira, Isabel Cardoso, Maria Rosário Domingues, Rui Vitorino, Margarida Bastos, Guangyue Bai, Maria João Saraiva, Maria Rosário Almeida

Article Affiliation:

Grupo de Neurobiologia Molecular, Instituto de Biologia Molecular e Celular, 4150-180 Porto, Portugal.


More than 100 transthyretin (TTR) variants are associated with hereditary amyloidosis. Approaches for TTR amyloidosis that interfere with any step of the cascade of events leading to fibril formation have therapeutic potential. In this study we tested (-)-epigallocatechin-3-gallate (EGCG), the most abundant catechin of green tea, as an inhibitor of TTR amyloid formation. We demonstrate that EGCG binds to TTR "in vitro" and "ex vivo" and that EGCG inhibits TTR aggregation "in vitro" and in a cell culture system. These findings together with the low toxicity of the compound raise the possibility of using EGCG in a therapeutic approach for familial amyloidotic polyneuropathy, the most frequent form of hereditary TTR amyloidosis.

Study Type : Review

Print Options

Key Research Topics

Sayer Ji
Founder of GreenMedInfo.com

Subscribe to our informative Newsletter & get Nature's Evidence-Based Pharmacy

Our newsletter serves 500,000 with essential news, research & healthy tips, daily.

Download Now

500+ pages of Natural Medicine Alternatives and Information.

This website is for information purposes only. By providing the information contained herein we are not diagnosing, treating, curing, mitigating, or preventing any type of disease or medical condition. Before beginning any type of natural, integrative or conventional treatment regimen, it is advisable to seek the advice of a licensed healthcare professional.

© Copyright 2008-2021 GreenMedInfo.com, Journal Articles copyright of original owners, MeSH copyright NLM.