Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry

Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry

Chiral inversion of amino acids is thought to modulate the structure and function of amyloid beta (Aβ) but these processes are poorly understood. Here, the authors develop an ion mobility-mass spectrometry based approach to study chirality-regulated structural features of Aβ fragments and their infl...

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Main Authors: Gongyu Li, Kellen DeLaney, Lingjun Li
Format: Article
Language:English
Published: Nature Publishing Group 2019-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-12346-8
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spelling doaj-e1966d5c12e14ee2889bec41b268dddb2021-05-11T11:51:23ZengNature Publishing GroupNature Communications2041-17232019-11-0110111110.1038/s41467-019-12346-8Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometryGongyu Li0Kellen DeLaney1Lingjun Li2School of Pharmacy, University of Wisconsin-MadisonDepartment of Chemistry, University of Wisconsin-MadisonSchool of Pharmacy, University of Wisconsin-MadisonChiral inversion of amino acids is thought to modulate the structure and function of amyloid beta (Aβ) but these processes are poorly understood. Here, the authors develop an ion mobility-mass spectrometry based approach to study chirality-regulated structural features of Aβ fragments and their influence on receptor recognition.https://doi.org/10.1038/s41467-019-12346-8
collection DOAJ
language English
format Article
sources DOAJ
author Gongyu Li
Kellen DeLaney
Lingjun Li
spellingShingle Gongyu Li
Kellen DeLaney
Lingjun Li
Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
Nature Communications
author_facet Gongyu Li
Kellen DeLaney
Lingjun Li
author_sort Gongyu Li
title Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
title_short Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
title_full Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
title_fullStr Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
title_full_unstemmed Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
title_sort molecular basis for chirality-regulated aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-11-01
description Chiral inversion of amino acids is thought to modulate the structure and function of amyloid beta (Aβ) but these processes are poorly understood. Here, the authors develop an ion mobility-mass spectrometry based approach to study chirality-regulated structural features of Aβ fragments and their influence on receptor recognition.
url https://doi.org/10.1038/s41467-019-12346-8
work_keys_str_mv AT gongyuli molecularbasisforchiralityregulatedabselfassemblyandreceptorrecognitionrevealedbyionmobilitymassspectrometry
AT kellendelaney molecularbasisforchiralityregulatedabselfassemblyandreceptorrecognitionrevealedbyionmobilitymassspectrometry
AT lingjunli molecularbasisforchiralityregulatedabselfassemblyandreceptorrecognitionrevealedbyionmobilitymassspectrometry
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