Abstract
Ambient surface mass spectrometry encompasses a broad range of sampling and ionization techniques. To date, only a small subset of these, based on liquid microjunction extraction, have proven suitable for intact protein analysis from thin tissue sections. Liquid extraction surface analysis shows particular promise for this application. Recently, a range of ion mobility spectrometry approaches have been coupled with ambient mass spectrometry. Improvements in signal-to-noise ratios, decreased chemical noise and separation of molecular classes have been described for the analysis of various biological substrates. Similar benefits have been described for ambient mass spectrometry imaging studies. In this review, we discuss the application of ambient mass spectrometry and ion mobility spectrometry to the analysis of intact proteins, and discuss opportunities and challenges for the field.
Highlights
Ambient ionization (AI) mass spectrometry (MS) refers to a range of techniques which enable the direct analysis of sample surfaces under ambient conditions [1]
Ambient ionization mass spectrometry offers a number of benefits for intact proteins over the traditional alternative of matrix-assisted laser desorption/ionization (MALDI)
This review focuses on the application of ambient ionization mass spectrometry for the analysis of intact proteins
Summary
Ambient ionization (AI) mass spectrometry (MS) refers to a range of techniques which enable the direct analysis of sample surfaces under ambient conditions [1]. Schematics of ambient ionization mass spectrometry techniques (a) desorption electrospray ionization (DESI), (b) liquid extraction surface analysis (LESA), (c) flowprobe sampling and (d) nano-DESI. Analysis of intact proteins by ambient mass spectrometry is largely confined to liquid microjunction surface-sampling (LMJ-SS) coupled to electrospray ionization (ESI). Travelling wave ion mobility spectrometry (TWIMS) has been coupled with DESI for the reduction of spectral complexity and simplification of data analysis in the imaging of multiply-charged gangliosides from murine brain tissue [89] and pharmaceutical tablets and preparations [90]. When compared with LESA mass spectrometry imaging in the absence of FAIMS, a wider range of intact protein species were detected owing to reduced chemical noise combined with improved signal-to-noise ratios. Similar benefits of FAIMS were reported via Flowprobe MSI (630 mm resolution) of intact proteins from murine brain and human ovarian cancer tissue [60]
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