Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue

Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new technique...

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Veröffentlicht in:Journal of the American Chemical Society 2023-07, Vol.145 (29), p.15658-15662
Hauptverfasser: Sisley, Emma K., Hale, Oliver J., Hughes, James W., Cooper, Helen J.
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container_issue 29
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container_title Journal of the American Chemical Society
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creator Sisley, Emma K.
Hale, Oliver J.
Hughes, James W.
Cooper, Helen J.
description Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new techniques that enable analysis of membrane proteins. Here we demonstrate native ambient mass spectrometry of membrane proteins, including β-barrel and α-helical (single and multipass) integral membrane proteins and membrane-associated proteins incorporating lipid anchors, by integration of a simple washing protocol to remove soluble proteins. Mass spectrometry imaging revealed that washing did not disrupt the spatial distributions of the membrane and membrane-associated proteins. Some delocalization of the remaining soluble proteins was observed.
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Mass Spectrometry - methods
Membrane Proteins - chemistry
title Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue
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