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NPRP grant from the Qatar National Research Fund (a member of the Qatar Foundation) [grant number NPRP8-425-1-087 ]

Authors

Publications

Role of aromatic amino acids in amyloid self-assembly

Stanković, Ivana M.; Niu, Shuqiang; Hall, Michael B.; Zarić, Snežana D.

(Elsevier, 2020)

TY  - JOUR
AU  - Stanković, Ivana M.
AU  - Niu, Shuqiang
AU  - Hall, Michael B.
AU  - Zarić, Snežana D.
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4176
AB  - 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.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Role of aromatic amino acids in amyloid self-assembly
VL  - 156
SP  - 949
EP  - 959
DO  - 10.1016/j.ijbiomac.2020.03.064
ER  - 
@article{
author = "Stanković, Ivana M. and Niu, Shuqiang and Hall, Michael B. and Zarić, Snežana D.",
year = "2020",
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.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Role of aromatic amino acids in amyloid self-assembly",
volume = "156",
pages = "949-959",
doi = "10.1016/j.ijbiomac.2020.03.064"
}
Stanković, I. M., Niu, S., Hall, M. B.,& Zarić, S. D.. (2020). Role of aromatic amino acids in amyloid self-assembly. in International Journal of Biological Macromolecules
Elsevier., 156, 949-959.
https://doi.org/10.1016/j.ijbiomac.2020.03.064
Stanković IM, Niu S, Hall MB, Zarić SD. Role of aromatic amino acids in amyloid self-assembly. in International Journal of Biological Macromolecules. 2020;156:949-959.
doi:10.1016/j.ijbiomac.2020.03.064 .
Stanković, Ivana M., Niu, Shuqiang, Hall, Michael B., Zarić, Snežana D., "Role of aromatic amino acids in amyloid self-assembly" in International Journal of Biological Macromolecules, 156 (2020):949-959,
https://doi.org/10.1016/j.ijbiomac.2020.03.064 . .
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