The way that amyloid beta (Aß) peptide is deposited into insoluble plaques in Alzheimer's disease is still unknown. There is some evidence that apolipoprotein E (apoE) binds to Aß peptide and modulates its aggregation into plaques. ApoE has three isoforms, apoE2, apoE3 and apoE4, and reports have shown that each apoE form may affect Aß aggregation in a specific manner. It has been suggested that apoE4 increases amyloid deposition, and it is commonly accepted that the conversion of Aß protein from a soluble form to an insoluble aggregate is associated with a structural or conformational change in the protein. The Aß peptide changes from an alpha-helix random coil form to a beta sheet structure. Dr. Wang suggests that apoE may play an important role in this conversion. He is using nuclear magnetic resonance (NMR) techniques to study the binding of Aß and apoE and the subsequent conformational changes to Aß. The primary goal of this project is to determine if apoE serves to promote or inhibit Aß conversion to the aggregated insoluble form. This could lead to developing inhibitors for Aß peptide aggregation and, ultimately, to better treatments or even a way to prevent AD.
First published on: June 10, 2008
Last modified on: June 11, 2008