Resolution and Assignment of Differential Ion Mobility Spectra of Sarcosine and Isomers

  • Francis Berthias
  • Belkis Maatoug
  • Gary L. Glish
  • Fathi Moussa
  • Philippe Maitre
Research Article


Due to their central role in biochemical processes, fast separation and identification of amino acids (AA) is of importance in many areas of the biomedical field including the diagnosis and monitoring of inborn errors of metabolism and biomarker discovery. Due to the large number of AA together with their isomers and isobars, common methods of AA analysis are tedious and time-consuming because they include a chromatographic separation step requiring pre- or post-column derivatization. Here, we propose a rapid method of separation and identification of sarcosine, a biomarker candidate of prostate cancer, from isomers using differential ion mobility spectrometry (DIMS) interfaced with a tandem mass spectrometer (MS/MS) instrument. Baseline separation of protonated sarcosine from α- and β-alanine isomers can be easily achieved. Identification of DIMS peak is performed using an isomer-specific activation mode where DIMS- and mass-selected ions are irradiated at selected wavenumbers allowing for the specific fragmentation via an infrared multiple photon dissociation (IRMPD) process. Two orthogonal methods to MS/MS are thus added, where the MS/MS(IRMPD) is nothing but an isomer-specific multiple reaction monitoring (MRM) method. The identification relies on the comparison of DIMS-MS/MS(IRMPD) chromatograms recorded at different wavenumbers. Based on the comparison of IR spectra of the three isomers, it is shown that specific depletion of the two protonated α- and β-alanine can be achieved, thus allowing for clear identification of the sarcosine peak. It is also demonstrated that DIMS-MS/MS(IRMPD) spectra in the carboxylic C=O stretching region allow for the resolution of overlapping DIMS peaks.

Graphical Abstract


Tandem mass spectrometry Ion mobility Differential ion mobility Infrared spectroscopy Quantum chemical calculations Amino acid Sarcosine Metabolomic 



We are thankful to the three reviewers for their constructive comments and suggestions.


This work is supported by a public grant from the “Laboratoire d’Excellence Physics Atom Light Mater” (LabEx PALM) overseen by the French National Research Agency (ANR) as part of the “Investissements d’Avenir” program (reference: ANR-10-LABX-0039). Financial support from the Centre National de la Recherche Scientifique (CNRS) is gratefully acknowledged.

Supplementary material

13361_2018_1902_MOESM1_ESM.docx (238 kb)
ESM 1 (DOCX 237 kb)


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Copyright information

© American Society for Mass Spectrometry 2018

Authors and Affiliations

  • Francis Berthias
    • 1
  • Belkis Maatoug
    • 1
  • Gary L. Glish
    • 2
  • Fathi Moussa
    • 3
    • 4
  • Philippe Maitre
    • 1
  1. 1.Laboratoire de Chimie Physique, Bâtiment 349Université Paris-Sud, CNRS, Université Paris-SaclayOrsayFrance
  2. 2.Department of Chemistry, Caudill LaboratoriesThe University of North Carolina at Chapel HillChapel HillUSA
  3. 3.Université Paris-Sud, LETIAM, Lip(Sys)2, IUT d’OrsayOrsayFrance
  4. 4.Biochemistry and Neuropediatric servicesHospital Group A. Trousseau-La Roche-Guyon, APHPParisFrance

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