Role of aromatic amino acids in amyloid self-assembly

Int J Biol Macromol. 2020 Aug 1:156:949-959. doi: 10.1016/j.ijbiomac.2020.03.064. Epub 2020 Mar 19.

Abstract

Amyloids are proteins of a cross-β structure found as deposits in several diseases and also in normal tissues (nails, spider net, silk). Aromatic amino acids are frequently found in amyloid deposits. Although they are not indispensable, aromatic amino acids, phenylalanine, tyrosine and tryptophan, enhance significantly the kinetics of formation and thermodynamic stability, while tape or ribbon-like morphology is represented in systems with experimentally detected π-π interactions between aromatic rings. Analysis of geometries and energies of the amyloid PDB structures indicate the prevalence of aromatic-nonaromatic interactions and confirm that aromatic-aromatic interactions are not crucial for the amyloid formation.

Keywords: Amyloids; Aromatic amino acids; Self-assembly.

Publication types

  • Review

MeSH terms

  • Amino Acids, Aromatic / chemistry*
  • Amyloid / chemistry*
  • Amyloid / ultrastructure
  • Amyloidogenic Proteins / chemistry
  • Animals
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Models, Molecular
  • Molecular Conformation
  • Protein Aggregates
  • Protein Aggregation, Pathological
  • Quantum Theory
  • Thermodynamics

Substances

  • Amino Acids, Aromatic
  • Amyloid
  • Amyloidogenic Proteins
  • Protein Aggregates