Aggregation of A(12-28) in the Presence of Ru3O clusters

Student Author(s)

Morgan Glover

Faculty Mentor(s)

Dr. Amanda Eckermann

Document Type


Event Date



Alzheimer’s disease (AD) is a neurodegenerative disease that affects more than 5 million Americans, and is currently the 6th leading cause of death in the United States. The A(1-42) protein is implicated in memory loss and degeneration of the brain in AD patients. The misfolding of the fragment A(12-28) is often studied to give insight into misfolding of the parent sequence, A (1-42). This fragment contains the hydrophobic KLVFFA section and the His residues, both of which are implicated in aggregation. A growing body of work shows that metal complexes with hydrophobic ligands are able to influence aggregation of A(1-42). We have prepared a library of hydrophobic Ru3O(OAc)6(L3)+/0 complexes where L = 4-phenlpyridine, pyridine, 4-dimethylaminopyridine, and isoquinoline. We are using label-free assays as well as fluorescent thioflavin T aggregation assays to investigate the effects of these Ru3O complexes on aggregation of A(12-28).

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