Distinguishing isomeric <i>N</i>-methylhistidine peptidoforms by ion mobility mass spectrometry

Histidine residues in proteins undergo histidine methyltransferase-catalysed Nτ-His and Nπ-His methylation. Here, we demonstrate that ion mobility spectrometry enables separation and identification of peptides possessing the isomeric Nτ-methyl-His and Nπ-methyl-His residues, leading to the assignment of the naturally occurring methyl-His isomer.

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Publication Details

Journal
Chemical Communications
Published
2025-01-01
DOI
https://doi.org/10.1039/d5cc03712c
Citations
3
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
Field-Weighted Citation Impact
2.27
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article

Distinguishing isomeric N-methylhistidine peptidoforms by ion mobility mass spectrometry

Janina Kamińska, Jasmin Mecinović, Nurgül Bilgin, Ole N. Jensen et al.
3 citations
Chemical Communications
Mass Spectrometry Techniques and Applications
2.27
article

Distinguishing isomeric N-methylhistidine peptidoforms by ion mobility mass spectrometry

Janina Kamińska, Jasmin Mecinović, Nurgül Bilgin, Ole N. Jensen, Tina Ravnsborg, Jakub Drożak, Francis Berthias, Paulina Emmel, Shah Adil Ishtiyaq Ahmad
article en
3 citations

Abstract

Histidine residues in proteins undergo histidine methyltransferase-catalysed Nτ-His and Nπ-His methylation. Here, we demonstrate that ion mobility spectrometry enables separation and identification of peptides possessing the isomeric Nτ-methyl-His and Nπ-methyl-His residues, leading to the assignment of the naturally occurring methyl-His isomer.

Chemical CommunicationsVol. 61(69)
University of Southern Denmark (DK), University of Warsaw (PL)
Openalex Percentile: Top 12%
Mass Spectrometry Techniques and Applications
2.27
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