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

Citations Over TimeTop 15% of 2018 papers

Abstract

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. The occurrence of this and other ordered structures increases at higher temperatures. At lower temperatures our binary mixture simulations indicate that increasing tryptophan content drives the assembly process away from the formation of distinct nanostructures and toward disordered aggregates which is in line with experimental observations of pure tryptophan solutions. This work provides molecular level insight to a variety of different physical phenomena relevant to fields including human disease.

Related Papers

• → YddG fromEscherichia colipromotes export of aromatic amino acids(2007)104 cited
• → Thermal Degradation of Aromatic Amino Acids(1971)27 cited
• → Transport of Aromatic Amino Acids by Pseudomonas aeruginosa(1971)31 cited
• → Thermal Degradation of Aromatic Amino Acids(1971)13 cited
• → Effect of aromatic acids on the influx of aromatic amino acids in rat brain slices(1977)14 cited