Interaction studies of amyloid beta-peptide with the natural compound resveratrol

• Tipo: Artigo em Livro de Atas de Conferência Internacional
• Data: 2015

Autores

Stephanie Andrade (Autor) Outra; Joana A. Loureiro (Autor) FEUP; Manuel A. N. Coelho (Autor) Outra; Maria do Carmo Pereira (Autor) Outra

Ata de Conferência Internacional

Título: Proceedings - 2015 IEEE 4th Portuguese Meeting on Bioengineering, ENBENG 2015

Páginas: 1-3

2015 4th IEEE Portuguese Meeting on Bioengineering, ENBENG 2015

26 February 2015 through 28 February 2015

Indexação

ISI Web of Knowledge - 1 Citação

Scopus - 7 Citações

INSPEC

Outras Informações

ID Authenticus: P-00G-4SN

DOI: 10.1109/enbeng.2015.7088833

Abstract (EN): The amyloid cascade hypothesis suggests that dysfunction and neuronal death in the brain is caused by the deposition of amyloid beta-peptide (A beta) in the Alzheimer's disease (AD). The peptide is aggregated as amyloid fibrils within the neuritic plaques and vascular deposits that characterize the disease. Thus, it is essential to find molecules that prevent or interrupt this aggregation process. Various natural compounds have been suggested as therapeutics for AD. Among these compounds, resveratrol (RES) arouses great interest in the therapy of AD. In this study the structure and fibril assembly of the A beta((1-42)) were analyzed in the presence of different sources of RES. The results demonstrated that A beta((1-42)) forms fibrils with different morphologies depending on the RES provenience. Moreover, TEM analysis and Thioflavin T fluorescence assay suggest that the presence of the resveratrol present in the grape skin retards or even inhibits the aggregation of the peptide.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 3