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Linda Broadbelt

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Ashty Karim

Neil Kelleher

The Kelleher Group pioneers cutting-edge technologies for understanding the role of proteins in health and disease and design-build-test cycles for creating synthetic protein-based drugs and diagnostics.

Analysis of whole protein molecules provides the ability to examine protein sequences, mutations, and modifications in unprecedented detail. Proteoforms, or all of the different molecular forms in which a protein can be found, capture all sources of protein variability (i.e., isoforms, SNPs, post-translational modifications, etc.), and thus provide crucial insights into biological function by connecting primary sequence and post-translational modifications. After a breakthrough Nature paper in 2011, Kelleher has continued to push the boundaries of proteomics, most recently culminating in a publication in Science (2022, 375: 411-418). Perspectives published by Kelleher and a consortium of like-minded researchers over the last decade articulating the value of proteoforms and a landmark project to map all proteoforms in the human body (Sci. Adv. 2021, 7: eabk0734) typify their thought leadership in a field seeing a new crescendo of interest and activity in the 2020s.

This ‘top-down’ approach to proteomics has propelled rapid development of new instrumentation and technologies for ultra-high performance mass spectrometry and uncovered new insights on clinically relevant protein targets such as KRAS (Ntai et al., PNAS, 2018) and ApoA-1 (Seckler et al., J Proteome Res., 2018).

‘Native’ top-down proteomics allows faithful preservation of post-translational modifications and non-covalent interactions in protein complexes and bioassemblies. This approach enables characterization of large virus-like capsids and their payloads (Kafader et al., Nature Methods, 2020) and endogenous and synthetic nucleosomes (Schachner et al., Nature Methods, 2021).

View Neil’s College of Arts and Sciences profile

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