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

Abstract

The amyloid cascade hypothesis suggests that dysfunction and neuronal death in the brain is caused by the deposition of amyloid beta-peptide (Aβ) 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 Aβ(1-42) were analyzed in the presence of different sources of RES. The results demonstrated that Aβ(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.