• Início
  • Resultados da busca
  • Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation.

Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation.

Biochimica et biophysica acta (2014-04-29)
Yanqin Liu, John A Carver, Antonio N Calabrese, Tara L Pukala
RESUMO

The accumulation of protein aggregates containing amyloid fibrils, with α-synuclein being the main component, is a pathological hallmark of Parkinson's disease (PD). Molecules which prevent the formation of amyloid fibrils or disassociate the toxic aggregates are touted as promising strategies to prevent or treat PD. In the present study, in vitro Thioflavin T fluorescence assays and transmission electron microscopy imaging results showed that gallic acid (GA) potently inhibits the formation of amyloid fibrils by α-synuclein. Ion mobility-mass spectrometry demonstrated that GA stabilises the extended, native structure of α-synuclein, whilst NMR spectroscopy revealed that GA interacts with α-synuclein transiently.

MATERIAIS
Número do produto
Marca
Descrição do produto

Sigma-Aldrich
Gallic acid, 97.5-102.5% (titration)
Sigma-Aldrich
Thioflavin T, used as stain for amyloid
Supelco
Gallic acid, certified reference material, TraceCERT®
Sigma-Aldrich
Thioflavine S, practical grade