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

• Type: Article in International Conference Proceedings Book
• Date: 2015

Authors

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

Conference proceedings International

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

Pages: 1-3

2015 4th IEEE Portuguese Meeting on Bioengineering, ENBENG 2015

26 February 2015 through 28 February 2015

Indexing

ISI Web of Knowledge - 1 Citation

Scopus - 7 Citations

INSPEC

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 3