Native ambient mass spectrometry: Latest developments for in situ protein analysis

Growing evidence suggests in situ protein analysis, i.e., directly from the physiological environment, has great potential for biomarker discovery, diagnosis & early detection of disease, targeting therapeutics (personalised medicine) and assessment of therapeutic efficacy. Mass spectrometry imaging (MSI) provides information on the spatial distribution of molecules within a biological substrate without the requirement for labelling. Its broad specificity, i.e., the capability to spatially profile any analyte ion detected, constitutes a major advantage over other imaging techniques. A separate branch of mass spectrometry, native mass spectrometry, provides information relating to protein structure through retention of solution-phase interactions in the gas-phase. Our research focuses on combining the benefits of MSI and native MS, i.e., to obtain information on both spatial distribution and tertiary or quaternary structure, through native mass spectrometry imaging (native MSI ).

Professor Helen J. Cooper is an expert in the gas-phase ion chemistry of peptides and proteins. She is a world-leader in the field of electron capture dissociation mass spectrometry and is responsible for establishing the University of Birmingham as a centre of excellence in mass spectrometry research. Professor Cooper has published extensively in peer-reviewed journals and serves on a number of national and international committees including the Editorial Board for the Journal of the American Society for Mass Spectrometry and the British Mass Spectrometry Society.

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Matt Humphries
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