Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy

Summary: We study the interaction between amyloid β (Aβ) peptides and Cu and Zn metal ions by using soft X-ray absorption spectroscopy. The spectral features of the peptides and Cu are simultaneously characterized by recording spectra at the N K-edge and at the Cu L2,3-edges. In the presence of the...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jinghui Luo, Hongzhi Wang, Jinming Wu, Vladyslav Romankov, Niéli Daffé, Jan Dreiser
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Organometallic chemistry Physical chemistry Biophysical chemistry Biochemistry Science Q
Acceso en línea:	https://doaj.org/article/823d241a313441ca8c0f59d8cfa95ae1
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:823d241a313441ca8c0f59d8cfa95ae1
record_format	dspace
spelling	oai:doaj.org-article:823d241a313441ca8c0f59d8cfa95ae12021-11-28T04:36:59ZAmyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy2589-004210.1016/j.isci.2021.103465https://doaj.org/article/823d241a313441ca8c0f59d8cfa95ae12021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S258900422101436Xhttps://doaj.org/toc/2589-0042Summary: We study the interaction between amyloid β (Aβ) peptides and Cu and Zn metal ions by using soft X-ray absorption spectroscopy. The spectral features of the peptides and Cu are simultaneously characterized by recording spectra at the N K-edge and at the Cu L2,3-edges. In the presence of the peptides, the Cu L2,3-edge shows a fingerprint of monovalent Cu(I), caused by the interaction with the peptides. The appearance of Cu(I) is less significant at an acidic pH than at a basic pH. Furthermore, aggregation leads to a smaller signature of Cu(I). N K-edge spectra reveal that Cu and Zn ions exhibit a different coordination with the nitrogen atoms in the peptides. This suggests different roles of Cu and Zn in the peptide aggregation. Our work provides physical insight into the participation of the metal ions and Aβ in the toxic reactive oxygen species formation.Jinghui LuoHongzhi WangJinming WuVladyslav RomankovNiéli DafféJan DreiserElsevierarticleOrganometallic chemistryPhysical chemistryBiophysical chemistryBiochemistryScienceQENiScience, Vol 24, Iss 12, Pp 103465- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Organometallic chemistry Physical chemistry Biophysical chemistry Biochemistry Science Q
spellingShingle	Organometallic chemistry Physical chemistry Biophysical chemistry Biochemistry Science Q Jinghui Luo Hongzhi Wang Jinming Wu Vladyslav Romankov Niéli Daffé Jan Dreiser Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
description	Summary: We study the interaction between amyloid β (Aβ) peptides and Cu and Zn metal ions by using soft X-ray absorption spectroscopy. The spectral features of the peptides and Cu are simultaneously characterized by recording spectra at the N K-edge and at the Cu L2,3-edges. In the presence of the peptides, the Cu L2,3-edge shows a fingerprint of monovalent Cu(I), caused by the interaction with the peptides. The appearance of Cu(I) is less significant at an acidic pH than at a basic pH. Furthermore, aggregation leads to a smaller signature of Cu(I). N K-edge spectra reveal that Cu and Zn ions exhibit a different coordination with the nitrogen atoms in the peptides. This suggests different roles of Cu and Zn in the peptide aggregation. Our work provides physical insight into the participation of the metal ions and Aβ in the toxic reactive oxygen species formation.
format	article
author	Jinghui Luo Hongzhi Wang Jinming Wu Vladyslav Romankov Niéli Daffé Jan Dreiser
author_facet	Jinghui Luo Hongzhi Wang Jinming Wu Vladyslav Romankov Niéli Daffé Jan Dreiser
author_sort	Jinghui Luo
title	Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
title_short	Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
title_full	Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
title_fullStr	Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
title_full_unstemmed	Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy
title_sort	amyloid-beta–copper interaction studied by simultaneous nitrogen k and copper l2,3-edge soft x-ray absorption spectroscopy
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/823d241a313441ca8c0f59d8cfa95ae1
work_keys_str_mv	AT jinghuiluo amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy AT hongzhiwang amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy AT jinmingwu amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy AT vladyslavromankov amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy AT nielidaffe amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy AT jandreiser amyloidbetacopperinteractionstudiedbysimultaneousnitrogenkandcopperl23edgesoftxrayabsorptionspectroscopy
_version_	1718408269995704320

Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3-edge soft X-ray absorption spectroscopy

Ejemplares similares