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Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation

Title
Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
Type
Article in International Scientific Journal
Year
2011
Authors
Nelson Ferreira
(Author)
Other
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Maria Joao Saraiva
(Author)
ICBAS
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Maria Rosario Almeida
(Author)
ICBAS
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Journal
Title: FEBS LettersImported from Authenticus Search for Journal Publications
Vol. 585
Pages: 2424-2430
ISSN: 0014-5793
Publisher: Wiley-Blackwell
Scientific classification
FOS: Natural sciences > Biological sciences
Other information
Authenticus ID: P-002-PBN
Abstract (EN): Several natural polyphenols with potent inhibitory effects on amyloid fibril formation have been reported. Herein, we studied modulation of transthyretin (TTR) fibrillogenesis by selected polyphenols. We demonstrate that both curcumin and nordihydroguaiaretic acid (NDGA) bind to TTR and stabilize the TTR tetramer. However, while NDGA slightly reduced TTR aggregation, curcumin strongly suppressed TTR amyloid fibril formation by generating small "off-pathway'' oligomers and EGCG maintained most of the protein in a non-aggregated soluble form. This indicates alternative mechanisms of action supported by the occurrence of different non-toxic intermediates. Moreover, EGCG and curcumin efficiently disaggregated pre-formed TTR amyloid fibrils. Our studies, together with the safe toxicological profile of these phytochemicals may guide a novel pharmacotherapy for TTR-related amyloidosis targeting different steps in fibrillogenesis. Structured summary of protein interactions: TTR binds to TTR by comigration in gel electrophoresis (View interaction) TTR binds to TTR by dynamic light scattering (View interaction) TTR binds to TTR by electron microscopy (View interaction)
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 7
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