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

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Nelson Ferreira (Author) Other; Isabel Cardoso (Author) Other; Maria Rosario Domingues (Author) Other; Rui Vitorino (Author) Other; Margarida Bastos (Author) FCUP; Guangyue Y Bai (Author) Other; Maria Joao Saraiva (Author) ICBAS; Maria Rosario Almeida (Author) ICBAS

Journal

Title: FEBS Letters

Vol. 583 No. 22

Pages: 3569-3576

ISSN: 0014-5793

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 112 Citations

Scopus - 114 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-003-EAZ

DOI: 10.1016/j.febslet.2009.10.062

Abstract (EN): 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 (uniprotkb:P02766) bind (MI:0407) by comigration in non-denaturing gel electrophoresis (MI:0404)

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8