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Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity |
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| Authors: | Nelson Ferreira Isabel Cardoso Rui Vitorino Guangyue Bai Maria Rosário Almeida |
| Institution: | a Grupo de Neurobiologia Molecular, IBMC - Instituto de Biologia Molecular e Celular, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal b Departamento de Biologia Molecular, ICBAS - Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Largo Prof. Abel Salazar, 2, 4099-003 Porto, Portugal c Centro de Espectrometria de Massa, Departamento de Química, Universidade de Aveiro, Campus Santiago, 3810-193 Aveiro, Portugal d Centro de Investigação em Química (UP) - CIQ (UP), Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, 687, P-4169-007 Porto, Portugal |
| Abstract: | 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 summaryMINT-7294529: TTR (uniprotkb:P02766) and TTR (uniprotkb:P02766) bind (MI:0407) by comigration in non-denaturing gel electrophoresis (MI:0404) |
| Keywords: | TTR transthyretin T4 thyroxine EGCG (&minus )-Epigallocatechin-3-gallate FAP familial amyloidotic polyneuropathy |
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