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Related Experiment Video

Updated: Jun 21, 2025

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
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Enhanced Declustering Enables Native Top-Down Analysis of Membrane Protein Complexes using Ion-Mobility Time-Aligned

Kleitos Sokratous1, Dale A Cooper-Shepherd2, Jakub Ujma2

  • 1OMass Therapeutics, Chancellor Court, John Smith Drive, ARC Oxford OX4 2GX, United Kingdom.

Journal of the American Society for Mass Spectrometry
|July 15, 2024
PubMed
Summary

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This study introduces an enhanced declustering device for native mass spectrometry, improving the analysis of complex protein interactions. This innovation aids in identifying novel drug compounds by enabling clearer protein-ligand complex analysis.

Area of Science:

  • Biochemistry and Biophysics
  • Analytical Chemistry
  • Structural Biology

Background:

  • Native mass spectrometry (MS) is crucial for studying protein interactions and functions.
  • Analyzing membrane proteins and screening compound libraries with native MS yields complex spectra.
  • Unambiguous peak assignment in native MS requires native top-down analysis, necessitating detergent removal.

Purpose of the Study:

  • To develop a method for improved native mass spectrometry analysis of complex protein samples.
  • To enable efficient detergent removal and isolation of protein-ligand complexes for top-down analysis.
  • To facilitate the identification of novel therapeutic targets and drug compounds.

Main Methods:

  • Implementation of a novel enhanced declustering (ED) device in a cyclic ion mobility spectrometry (IMS)-enabled mass spectrometry platform.
Keywords:
ion-mobility spectrometrymembrane proteinnative mass spectrometrytop down

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Last Updated: Jun 21, 2025

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  • Utilizing an oscillating electric field for ion declustering and liberation of membrane proteins from detergent micelles.
  • Employing quadrupole selection for isolating protein-ligand complexes and collision-induced dissociation for fragmentation.

    • Main Results:

    • The ED device effectively declusters ions and liberates membrane proteins prior to MS analysis.
    • Ion mobility (IM) significantly aids in assigning top-down spectra by correlating fragments with parent ions via drift time.
    • Successful identification of a novel hit compound against PfMATE from multiplexed ligand libraries.

    Conclusions:

    • The novel ED device enhances native MS capabilities for analyzing complex protein assemblies and interactions.
    • This approach simplifies the interpretation of complex spectra, enabling unambiguous peak assignment in top-down analysis.
    • The developed method facilitates drug discovery by enabling efficient screening and identification of protein-ligand interactions.