Trinuclear Ruthenium Acetate Clusters as Structural Disruptors for A(1-42)

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) amyloid protein is implicated in memory loss and degeneration of the brain in AD patients. The misfolding of this protein can cause it to oligomerize, form insoluble plaques, and interfere with normal neuronal activities in the brain. Previous researchers have shown that the short peptide KLVFFA inhibits the oligomerization of A(1-42). We have designed a trinuclear ruthenium complex to incorporate a KLVFFAH ligand to target A(1- 42) and interfere with oligomerization. We have prepared several clusters of the formula Ru3O(OAc)6(L3)+, where L is a series of N-heterocycles. Further, previous work has found that insulin aggregates in a manner analogous to the A(1-42) protein. We have investigated the effects of Ru3O(L)3 compounds on aggregation of insulin fibrils.


This research was supported by the Natural and Applied Sciences Division of Hope College.

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