The amyloid beta (Aβ) aggregation pathway is an important therapeutic target in the treatment of Alzheimer’s disease (AD). Amyloid-β fibrils, which are a major component of the plaques found in disease patients, are formed by the oligomerization of mixed length Aβ monomers. The neurotoxic species is thought to be a soluble oligomer of Aβ42, which can further aggregate to form an insoluble fibril that may not cause neural degeneration. Previous work has sought to inhibit aggregation by binding the monomeric species. In this study, the small molecule 2002-H20 was discovered as a direct binder of Aβ peptide (SMM). 2002-H20 was able to rescue cells from Aβ-induced toxicity in a dose dependent manner (MTT viability assay), and was shown to enhance fibril formation (electron microscopy, Congo red binding). This suggests that the mechanism of action of 2002-H20 may be to accelerate Aβ aggregation past the toxic soluble oligomer, rather than inhibit aggregation. Chen et al., J. Am. Chem. Soc., 132, 17015-17022, 2010.