ellagic-acid and Alzheimer-Disease

Amyloid β (Aβ) aggregates in the brains of patients with Alzheimer's disease (AD) and accumulates via oligomerization and subsequent fiber elongation processes. These toxicity-induced neuronal damage and shedding processes advance AD progression. Therefore, Aβ aggregation-inhibiting substances may contribute to the prevention and treatment of AD. We screened for Aβ42 aggregation inhibitory activity using various plant extracts and compounds, and found high activity for a Geranium thunbergii extract (EC

Topics: Alzheimer Disease; Amyloid; Amyloid beta-Peptides; Geranium; Humans; Neurons; Peptide Fragments; Plant Extracts

Polymerization of the amyloid beta-peptide (Abeta) has been identified as one of the major characteristics of Alzheimer's disease (AD). Thus, finding molecules to prevent the aggregation of Abeta could be of therapeutic value in AD. We describe an original routine in vitro assay to search for inhibitors of Abeta(25-35) fibril formation which uses UV-visible measurements and electron microscopy (EM). In particular, this routine assay was used to examine the effects of stilbenes, a well-known polyphenol class, as inhibitors of Abeta fibril formation. The inhibitory properties of resveratrol (RES), piceid (PIC), resveratrol diglucoside (DIG), piceatannol (PIA), astringine (AST), and viniferin (VIN) were characterized and compared. RES and PIC effectively and dose-dependently inhibited Abeta polymerization while other polyphenols exerted less inhibition. Although the mechanism of anti-amyloidogenic activity is still unknown, these results support the hypothesis that stilbenes could be of therapeutic value in AD.

Topics: Algorithms; Alzheimer Disease; Amyloid beta-Peptides; Animals; Bradykinin; Curcumin; Microscopy, Electron; PC12 Cells; Peptide Fragments; Polymers; Rats; Solutions; Spectrophotometry, Ultraviolet; Stilbenes