Journal article
Ion Mobility–Based Enrichment-Free N-Terminomics Analysis Reveals Novel Legumain Substrates in Murine Spleen
AR Ziegler, A Dufour, NE Scott, LE Edgington-Mitchell
Molecular and Cellular Proteomics | Published : 2024
Abstract
Aberrant levels of the asparaginyl endopeptidase legumain have been linked to inflammation, neuro-degeneration, and cancer, yet our understanding of this protease is incomplete. Systematic attempts to identify legumain substrates have been previously confined to in vitro studies, which fail to mirror physiological conditions and obscure biologically relevant cleavage events. Using high-field asymmetric waveform ion mobility spectrometry (FAIMS), we developed a streamlined approach for proteome and N-terminome analyses without the need for N-termini enrichment. Compared to unfractionated proteomic analysis, we demonstrate FAIMS fractionation improves N-termini identification by >2.5 fold, res..
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Awarded by Australian Government
Funding Acknowledgements
L. E. E.-M. was sup-ported by a Grimwade Fellowship funded by the Russell and Mab Grimwade Miegunyah Fund at the University of Melbourne, a DECRA Fellowship from the Australian Research Council (ARC, DE180100418) , and a grant from the National Health and Medical Research Council (NHMRC, GNT2011119) . N. E. S is supported by an ARC Future Fellowship (FT200100270) , an ARC Discovery Project Grant (DP210100362) , and an NHMRC Ideas grant (2018980) . A. R. Z. was supported by an RTP Scholarship from the Australian Government.