NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations

Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane d...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Minseon Kim, Jinyoung Son, Yongae Kim
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	amyloid channel transmembrane protein Alzheimer’s disease solution-state NMR solid-state NMR Chemical technology TP1-1185 Chemical engineering TP155-156
Acceso en línea:	https://doaj.org/article/72b3b0ddedf04517b262ae1104939e65
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:72b3b0ddedf04517b262ae1104939e65
record_format	dspace
spelling	oai:doaj.org-article:72b3b0ddedf04517b262ae1104939e652021-11-25T18:19:26ZNMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations10.3390/membranes111107992077-0375https://doaj.org/article/72b3b0ddedf04517b262ae1104939e652021-10-01T00:00:00Zhttps://www.mdpi.com/2077-0375/11/11/799https://doaj.org/toc/2077-0375Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of Aβ ion channels. In addition, various studies have investigated substances that block or inhibit the formation of Aβ ion channels. Zinc ions are considered as potential inhibitors of AD. In this study, we focused on the transmembrane domain and some external domains of the Aβ protein (hAPP-TM), and solution-state NMR was used to confirm the effect on residues of the protein in the presence of zinc ions. In addition, we sought to confirm the structure and orientation of the protein in the presence of the bicelle using solid-state NMR.Minseon KimJinyoung SonYongae KimMDPI AGarticleamyloid channeltransmembrane proteinAlzheimer’s diseasesolution-state NMRsolid-state NMRChemical technologyTP1-1185Chemical engineeringTP155-156ENMembranes, Vol 11, Iss 799, p 799 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	amyloid channel transmembrane protein Alzheimer’s disease solution-state NMR solid-state NMR Chemical technology TP1-1185 Chemical engineering TP155-156
spellingShingle	amyloid channel transmembrane protein Alzheimer’s disease solution-state NMR solid-state NMR Chemical technology TP1-1185 Chemical engineering TP155-156 Minseon Kim Jinyoung Son Yongae Kim NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
description	Alzheimer’s disease (AD) is classified as an amyloid-related disease. Amyloid beta (Aβ) is a transmembrane protein known to play a major role in the pathogenesis of AD. These Aβ proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of Aβ ion channels. In addition, various studies have investigated substances that block or inhibit the formation of Aβ ion channels. Zinc ions are considered as potential inhibitors of AD. In this study, we focused on the transmembrane domain and some external domains of the Aβ protein (hAPP-TM), and solution-state NMR was used to confirm the effect on residues of the protein in the presence of zinc ions. In addition, we sought to confirm the structure and orientation of the protein in the presence of the bicelle using solid-state NMR.
format	article
author	Minseon Kim Jinyoung Son Yongae Kim
author_facet	Minseon Kim Jinyoung Son Yongae Kim
author_sort	Minseon Kim
title	NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
title_short	NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
title_full	NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
title_fullStr	NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
title_full_unstemmed	NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations
title_sort	nmr studies of the ion channel-forming human amyloid-β with zinc ion concentrations
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/72b3b0ddedf04517b262ae1104939e65
work_keys_str_mv	AT minseonkim nmrstudiesoftheionchannelforminghumanamyloidbwithzincionconcentrations AT jinyoungson nmrstudiesoftheionchannelforminghumanamyloidbwithzincionconcentrations AT yongaekim nmrstudiesoftheionchannelforminghumanamyloidbwithzincionconcentrations
_version_	1718411325935190016

NMR Studies of the Ion Channel-Forming Human Amyloid-β with Zinc Ion Concentrations

Ejemplares similares