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Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry

High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. P...

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Detalles Bibliográficos
Autores principales: Creese, Andrew J., Cooper, Helen J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088216/
https://www.ncbi.nlm.nih.gov/pubmed/27704474
http://dx.doi.org/10.1007/s13361-016-1482-1
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author Creese, Andrew J.
Cooper, Helen J.
author_facet Creese, Andrew J.
Cooper, Helen J.
author_sort Creese, Andrew J.
collection PubMed
description High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation—the PPI helix—in 1-propanol, and an all-trans conformation—the PPII helix—in aqueous solutions. Differentiation of these conformers may be achieved both through use of a cylindrical FAIMS device and a miniaturized ultrahigh field planar FAIMS device. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13361-016-1482-1) contains supplementary material, which is available to authorized users.
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spelling pubmed-50882162016-11-16 Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry Creese, Andrew J. Cooper, Helen J. J Am Soc Mass Spectrom Application Note High field asymmetric waveform ion mobility spectrometry (FAIMS) is well-established as a tool for separating peptide isomers (sequence inversions and post-translationally modified localization variants). Here, we demonstrate the FAIMS is able to differentiate cis and trans isomers of polyproline. Polyproline assumes an all-cis conformation—the PPI helix—in 1-propanol, and an all-trans conformation—the PPII helix—in aqueous solutions. Differentiation of these conformers may be achieved both through use of a cylindrical FAIMS device and a miniaturized ultrahigh field planar FAIMS device. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13361-016-1482-1) contains supplementary material, which is available to authorized users. Springer US 2016-10-04 2016 /pmc/articles/PMC5088216/ /pubmed/27704474 http://dx.doi.org/10.1007/s13361-016-1482-1 Text en © The Author(s) 2016 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Application Note
Creese, Andrew J.
Cooper, Helen J.
Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title_full Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title_fullStr Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title_full_unstemmed Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title_short Separation of cis and trans Isomers of Polyproline by FAIMS Mass Spectrometry
title_sort separation of cis and trans isomers of polyproline by faims mass spectrometry
topic Application Note
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5088216/
https://www.ncbi.nlm.nih.gov/pubmed/27704474
http://dx.doi.org/10.1007/s13361-016-1482-1
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