Structure determination of amyloid-β oligomers (40-, 42-residues) with AlphaFold2

Alzheimer's disease (AD) afflicts millions worldwide and its impact will only worsen as the population ages. One of the most important aspects of AD's pathogenesis is the aggregation of amyloid-β peptides into complexes of amyloid-β oligomers (AβOs). However, relatively little is known about AβOs as their instability makes them resistant to traditional imaging techniques. To elucidate AβOs, we used Alphafold-2.3.2's complex prediction algorithm for structure determination of 2- through 15-peptide AβOs using the most common pathogenic amyloid-β peptides (40-, and 42-residues).