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

作者：Ferreira Nelson; Cardoso Isabel; Domingues Maria Rosario; Vitorino Rui; Bastos Margarida; Bai Guangyue; Saraiva Maria Joao; Almeida Maria Rosario^*

来源：FEBS LETTERS, 2009, 583(22): 3569-3576.

DOI：10.1016/j.febslet.2009.10.062

• Transthyretin
• (-)-Epigallocatechin-3-gallate
• Amyloid
• Aggregation

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.
Structured summary:
MINT-7294529: TTR (uniprotkb:P02766) and TTR

• 出版日期2009-11-19