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Alzheimer's disease is a severe neurodegenerative disease characterized by the aggregation of amyloid- β  peptide (A β ) into toxic oligomers which activate microglia and astrocytes causing acute neuroinflammation. Multiple studies show that the soluble oligomers of A β 42 are neurotoxic and proinflammatory, whereas the monomers and insoluble fibrils are relatively nontoxic. We show that A β 42 aggregation is inhibited  in vitro  by oil palm phenolics (OPP), an aqueous extract from the oil palm tree  (Elaeis guineensis) . The data shows that OPP inhibits stacking of  β -pleated sheets, which is essential for oligomerization. We demonstrate the inhibition of A β 42 aggregation by (1) mass spectrometry; (2) Congo Red dye binding; (3) 2D-IR spectroscopy; (4) dynamic light scattering; (5) transmission electron microscopy; and (6) transgenic yeast rescue assay. In the yeast rescue assay, OPP significantly reduces the cytotoxicity of aggregating neuropeptides in yeast genetically engineered to overexpress these peptides. The data shows that OPP inhibits (1) the aggregation of A β  into oligomers; (2) stacking of  β -pleated sheets; and (3) fibrillar growth and coalescence. These inhibitory effects prevent the formation of neurotoxic oligomers and hold potential as a means to reduce neuroinflammation and neuronal death and thereby may play some role in the prevention or treatment of Alzheimer's disease.

Oil Palm Phenolics Inhibit theIn VitroAggregation ofβ-Amyloid Peptide into Oligomeric Complexes