Mass spectrometry imaging enables spatial distribution analysis of analytes across substrates such as thin tissue sections. Identifying and mapping analytes as a function of tissue location is used to evaluate biological hypotheses associating specific compounds with function and disease. MS-imaging is particularly attractive as it reduces sample handling, increases acquisition speed across hundreds of spots on the tissue, can simultaneously map large numbers of analytes within a full mass spectrum, and perform tandem MS within a minute per spot. The challenge, however, is successfully detecting, characterizing, and spatially profiling protein/proteoforms due to the low amounts of sample and spectral complexity within a small pixel on the tissue slice.
In this webcast, the speaker will discuss a novel workflow for spatial profiling of intact proteins on tissue slices utilizing native LESA MS to identify larger proteins (>47 kDa) than previous research, as well as detecting and characterizing protein complexes with molecular weights ca. 103 kDa, demonstrating the softness of the ionization and transmission of protein complexes through FAIMS. Higher order MSn is performed to dissociate the complexes into subgroups, and sequence subgroups using multiple dissociation techniques. Combining FAIMS with LESA MS has enabled detection of hundreds of proteins in human liver sections.
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