Spatial omic measurements provide invaluable information on cellular organization and interactions in native tissues, organs, and communities. While single-cell DNA/RNA sequencing have dramatically advanced our understanding of cellular diversity and heterogeneity, these technologies capture only a partial picture of a cell’s phenotype. Proteins and proteoforms are of particular interest in establishing cellular identities because they are the primary effectors of biological function, and their modification state or abundance cannot be easily inferred from sequencing measurements. However, the ability to measure proteins and proteoforms in a few cells or a single cell is a major analytical challenge. Current approaches for probing spatial distribution of the proteome typically rely on the use of labels or antibodies, which limits multiplexing and requires a priori knowledge of protein targets. Conventional bottom-up proteomics has been demonstrated for proteome-wide analysis of small tissue sections. However, this approach cannot provide proteoform maps and is therefore lacking because proteoforms drive cellular functions. To address the proteoform mapping challenge with enhanced throughput and resolution, we integrated nanoPOTS top-down proteomics and MALDI mass spectrometry imaging. In this presentation we will demonstrate how advanced FTMS instrumentation and methods can map proteoforms in human organs at near single cell resolution.

Recent advances in spatial and cellular proteomics

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