Role of aromatic amino acids in amyloid self-assembly
Authorized Users Only
Article (Accepted Version)
MetadataShow full item record
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
Source:International Journal of Biological Macromolecules, 2020, 156, 949-959
- Noncovalent interactions of pi-systems and their role in molecular recognition (RS-172065)
- NPRP grant from the Qatar National Research Fund (a member of the Qatar Foundation) [grant number NPRP8-425-1-087].
- NSF (CHE-1664866)
- This is the peer-reviewed version of the article: Ivana M. Stanković, Shuqiang Niu, Michael B. Hall, Snežana D. Zarić, Role of aromatic amino acids in amyloid self-assembly, International Journal of Biological Macromolecules, 2020, 156, 949-959, https://doi.org/10.1016/j.ijbiomac.2020.03.064
- Published version: http://cer.ihtm.bg.ac.rs/handle/123456789/3606