Role of aromatic amino acids in amyloid self-assembly. Academic Article

abstract

• Amyloids are proteins of a cross- 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 - 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.

authors

• Hall, Michael

published proceedings

• Int J Biol Macromol

author list (cited authors)

• Stankovi, I. M., Niu, S., Hall, M. B., & Zari, S. D.

citation count

• 21

complete list of authors

• Stanković, Ivana M||Niu, Shuqiang||Hall, Michael B||Zarić, Snežana D

publication date

• August 2020

publisher

• Elsevier  Publisher

published in

• International Journal of Biological Macromolecules  Journal

keywords

• Amino Acids, Aromatic
• Amyloid
• Amyloidogenic Proteins
• Amyloids
• Animals
• Aromatic Amino Acids
• Humans
• Hydrophobic And Hydrophilic Interactions
• Kinetics
• Models, Molecular
• Molecular Conformation
• Protein Aggregates
• Protein Aggregation, Pathological
• Quantum Theory
• Self-assembly
• Thermodynamics

PubMed Central ID

• 32199918

Digital Object Identifier (DOI)

• 10.1016/j.ijbiomac.2020.03.064

start page

• 949

end page

• 959

volume

• 156

URL

• http://dx.doi.org/10.1016/j.ijbiomac.2020.03.064