Speaker
Description
The Omnitrap-Orbitrap-Booster (OOB) mass spectrometry (MS) platform with enhanced high-resolution, fragmentation and data acquisition capabilities, was developed to advance top-down (TD) MS analysis of proteins. It integrates a multimodal tandem mass spectrometry (MS/MS) ion trap system (OmnitrapTM) offering a wide range of fragmentation methods, a high-resolution Orbitrap Fourier transform mass spectrometer (FTMS), and a high-performance data acquisition system (FTMS Booster) to improve fragmentation efficiency and spectral quality by increasing the signal-to-noise (S/N) ratio of product ions. In this study, we evaluate the OOB platform for electron capture dissociation (ECD)-based TD MS analysis of a clinical multiple myeloma antibody light chain extracted from the patient’s (P15) urine sample, benchmarking its performance against the “gold-standard” electron transfer dissociation (ETD)-based TD MS on an Orbitrap EclipseTM. These analyses were performed with online coupling to a LC system operating in nanoflow mode. Comparable sequence coverage was obtained for single precursor charge state analysis between ECD-based TD MS on OOB and ETD-based TD MS on EclipseTM (68.2% vs. 74.3% respectively). ECD showed a lower spectral peak density and reduced redundancy of product ions. Moreover, the analysis of multiple precursor charge states (15+ to 19+) sequentially across 5 runs of LC-MS/MS on the OOB platform improves the sequence coverage to 93%, indicating its suitability for comprehensive characterization of protein. Thus, this study uniquely establishes the OOB platform as a highly powerful and efficient system for TD MS of proteins.
| User consent | yes |
|---|
