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:
Application Note
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
Descripción
Sumario: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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