Speaker
Description
More than 30 million individuals worldwide are living with Alzheimer’s Disease. To further the current understanding on this neurodegenerative disease, we developed a technique to create amyloid peptide clusters in synthetic, brain-like membranes, which mimic the senile plaques found in the brains of Alzheimer's patients. I compared the molecular functioning of homotaurine, a peptic anti-aggregant that binds to amyloid peptides directly, and curcumin, a non-peptic molecule that can inhibit aggregation by changing membrane properties. By using microscopy, x-ray diffraction, and UV-vis spectroscopy, we found that both curcumin and homotaurine significantly reduce the number of small, nanoscopic amyloid aggregates and the corresponding β- and cross-β sheet signals. This research shows that membrane active drugs can be as efficient as peptide targeting drugs in inhibiting amyloid aggregation in-vitro [1]. The findings can open new pathways for the developments of drugs to slow down first occurrence and progression of the disease.
[1] Xingyuan Zou, Sebastian Himbert, Janos Juhasz, Samantha Ros, Harald D. H. Stover, and Maikel C. Rheinstädter, “Curcumin and homotaurine suppress amyloid-b25-35 aggregation in synthetic brain membranes”, under review with ACS Chemical Neuroscience, Manuscript ID: cn-2021-00057r
