High levels of acrolein (H2C=HC-CH=O) occur in Alzheimer's brain. Amyloid-beta (A beta) peptide co-localizes with acrolein presumably due to A beta-induced lipid peroxidation. Focal production of acrolein may yield a transient elevation in the concentration of acrolein that may be susceptible to polymerization via basic latex polymer chemistry. Following incubation of A with acrolein (16-750 mM), we observed the formation of thin plastic fragments that were extensively punctuated. Planar aggregates stained for protein and for cross-P structures suggesting an A beta-polyacrolein colloidal mixture. Depending on acrolein concentration and incubation time, we observed uniformly sized planar aggregates (approximately 10 mu m(2)) or monolayers (> 100 mm(2)) of thin polyacrolein films embedded with A beta oligomers. The ability of A beta to catalyze the polymerization of acrolein is likely due to A beta's surfactant and redox properties. These observations suggest that plastic in the form of A beta-polyacrolein latexes may exist in neural tissue contributing to the pathogenesis of Alzheimer's disease. (c) 2005 Elsevier Inc. All rights reserved.