His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria

Abstract Oligomers of Aβ peptide are implicated as the most probable causative agent in Alzheimer’s disease. However, their structural properties remain elusive due to the dynamic and heterogeneous character of oligomeric species coexisting in solution. Nevertheless, new approaches, mainly based on...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Kaja Przygońska, Magdalena Pacewicz, Wiktoria Sadowska, Jarosław Poznański, Wojciech Bal, Michał Dadlez
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
Materias:
R
Q
Acceso en línea:https://doaj.org/article/7f3beb276d5440eb9a6d11c0aedd833e
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:7f3beb276d5440eb9a6d11c0aedd833e
record_format dspace
spelling oai:doaj.org-article:7f3beb276d5440eb9a6d11c0aedd833e2021-12-02T16:08:04ZHis6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria10.1038/s41598-019-45988-12045-2322https://doaj.org/article/7f3beb276d5440eb9a6d11c0aedd833e2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-45988-1https://doaj.org/toc/2045-2322Abstract Oligomers of Aβ peptide are implicated as the most probable causative agent in Alzheimer’s disease. However, their structural properties remain elusive due to the dynamic and heterogeneous character of oligomeric species coexisting in solution. Nevertheless, new approaches, mainly based on mass spectrometry, provide unique access to these different structural forms. Using these methods, we previously showed that the N-terminal, non-amyloidogenic region of Aβ is involved in the network of interactions specifically stabilizing oligomers. In the present study, we identified three histidine residues as active participants in this network. Detailed knowledge of the structural features that are potentially important for oligomer-mediated neurotoxicity is a prerequisite for the rational design of oligomerization modifiers.Kaja PrzygońskaMagdalena PacewiczWiktoria SadowskaJarosław PoznańskiWojciech BalMichał DadlezNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Kaja Przygońska
Magdalena Pacewicz
Wiktoria Sadowska
Jarosław Poznański
Wojciech Bal
Michał Dadlez
His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
description Abstract Oligomers of Aβ peptide are implicated as the most probable causative agent in Alzheimer’s disease. However, their structural properties remain elusive due to the dynamic and heterogeneous character of oligomeric species coexisting in solution. Nevertheless, new approaches, mainly based on mass spectrometry, provide unique access to these different structural forms. Using these methods, we previously showed that the N-terminal, non-amyloidogenic region of Aβ is involved in the network of interactions specifically stabilizing oligomers. In the present study, we identified three histidine residues as active participants in this network. Detailed knowledge of the structural features that are potentially important for oligomer-mediated neurotoxicity is a prerequisite for the rational design of oligomerization modifiers.
format article
author Kaja Przygońska
Magdalena Pacewicz
Wiktoria Sadowska
Jarosław Poznański
Wojciech Bal
Michał Dadlez
author_facet Kaja Przygońska
Magdalena Pacewicz
Wiktoria Sadowska
Jarosław Poznański
Wojciech Bal
Michał Dadlez
author_sort Kaja Przygońska
title His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
title_short His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
title_full His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
title_fullStr His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
title_full_unstemmed His6, His13, and His14 residues in Aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
title_sort his6, his13, and his14 residues in aβ 1–40 peptide significantly and specifically affect oligomeric equilibria
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/7f3beb276d5440eb9a6d11c0aedd833e
work_keys_str_mv AT kajaprzygonska his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
AT magdalenapacewicz his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
AT wiktoriasadowska his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
AT jarosławpoznanski his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
AT wojciechbal his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
AT michałdadlez his6his13andhis14residuesinab140peptidesignificantlyandspecificallyaffectoligomericequilibria
_version_ 1718384666363297792