Alzheimer’s disease is a neurodegenerative disease characterized by the formation of aggregated Aß peptide plaques in brain tissue. Several studies have shown that metal ions and free radical reactions can affect the disease process, including that Zn, Cu and Fe have effects on the amyloid aggregation kinetics of the Aß peptide.   These observations form the metal ion theory of Alzheimer’s disease and the development of “metal-protein attenuating compounds” (MPACs) for the treatment of Alzheimer’s disease.  The archetypal MPAC is Clioquinol (CQ), which along with various analogues, has been trailed in phase II clinical trials, showing several positive outcomes in both preventing loss of cognition and plaque formation.  The proposed mechanism of action of these compounds is an ionophore activity, which restores mislocalised metal ions to their appropriate locations and levels.  Despite the role of metals in the development of these compounds for Alzheimer’s disease, there is further evidence that hydroxyquionlines can bind Aß and affect its aggregation propensity directly. We characterized the potential direct interaction of CQ with Aß using a variety of biophysical techniques, and find that this interaction does occur with a stoichiometry of 1:1 and that it is metal independent. This interaction completely suppresses the formation of large soluble oligomers and stabilizes low n oligomers. In addition, this compound displays a similar anti-oligomer effect in the C. elegans worm model of Aß toxicity.  We propose that this activity is an additional mechanism of action, which may result in enhanced clearance of aggregated Aß from brain tissue.