From Quantum Mechanics, Classical Mechanics, and Bioinformatics to Artificial Intelligence Studies in Neurodegenerative Diseases.

The amyloid β-protein is an intrinsically disordered protein that has the potential to assemble into myriad structures, including oligomers and fibrils. These structures are neurotoxic and are thought to initiate a cascade of events leading to Alzheimer's disease. Understanding this pathogenetic process and elucidating targets for drug therapy depends on elucidation of the structural dynamics of Aβ assembly.

Self-assembly of aromatic amino acids: a molecular dynamics study.

The self assembly processes of aromatic amino acids, phenylalanine, tyrosine, and tryptophan have been simulated and were observed to form fibril-like aggregates linked to certain rare diseases and instances of biological membrane disruption. Pure systems and their mixtures were studied systematically at constant temperatures and free energy landscapes were produced describing the height and the number of assembled monomers associated with lower energy structures. Consistent with some previous work, aromatic amino acid monomers display a tendency to arrange with a four-fold symmetry.