Over the last few years, mass spectrometry based proteomics workflows have become increasingly more powerful in capturing complex proteomes to incredible depths. This has largely been driven by the adoption of data-independent acquisition (DIA) modes, where all incoming ions are repeatedly sampled at even times through the liquid chromatography run, providing a comprehensive fragmentation map of nearly all potential ions.
Here, Meier et al makes use of IonOpticks Aurora Series columns to demonstrate unprecedented proteomic depth using this new diaPASEF mode. The high correlation of molecular weight and ion mobility in a trapped ion mobility device (Bruker’s timsTOF Pro) facilitates sampling of near 100% of the peptide precursor ion current. Additionally, they establish a targeted data extraction workflow by inclusion of the ion mobility dimension which increases the specificity for precursor identification. Overall, the DIAPASEF acquisition mode in combination with Aurora series columns facilitates incredibly deep proteome coverage with a high degree of reproducibility and quantitative accuracy.
Read the full paper
diaPASEF: parallel accumulation–serial fragmentation combined with data-independent acquisition.
Nat Methods. 17, 1229–1236 (2020). doi: https://doi.org/10.1038/s41592-020-00998-0
Meier F, Brunner AD, Frank M, Ha A, Bludau I, Voytik E, Kaspar-Schoenefeld S, Lubeck M, Raether O, Bache N, Aebersold R, Collins BC, Röst HL and Mann M.
Commentary by Andrew Webb, PhD.
About the author
Andrew has over 15 years’ experience in the field of chromatography and mass spectrometry. He is the lead innovator and inventor at IonOpticks, working closely with the team to test, refine and develop cutting edge techniques to support higher quality outputs and analytics from MS instruments. Andrew is also the Lab Head of the Walter and Eliza Hall Institute of Medical Research’s Proteomics Research Laboratory.