Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins

Abstract

We describe an instrument configuration based on the Orbitrap Exploris 480 mass spectrometer that has been coupled to an Omnitrap platform. The Omnitrap possesses three distinct ion-activation regions that can be used to perform resonant-based collision-induced dissociation, several forms of electron-associated fragmentation, and ultraviolet photodissociation. Each section can also be combined with infrared multiphoton dissociation. In this work, we demonstrate all these modes of operation in a range of peptides and proteins. The results show that this instrument configuration produces similar data to previous implementations of each activation technique and at similar efficiency levels. We demonstrate that this unique instrument configuration is extremely versatile for the investigation of polypeptides.

Mass Spectrometry Investigation of Some ATP-Binding Cassette (ABC) Proteins

“…For instance, 193 nm was first applied in the 1980s [84,85]; however, such an application was limited to specific peptides performed on Fourier transform ion cyclotron resonance (FTICR) mass spectrometers. Over the last ten years and due to advances in UV lasers and in MS instrumentation, the technique has witnessed a resurgence, represented in its use in a wide range of instruments, including TOF [86], linear ion traps [87], and more recently in the orbitrap [88]. UVPD mainly uses two wave lengths, 157 and 193 nm; however, the wavelength 213 nm has been used to sequence intact proteoforms in top-down proteomics [89].…”

“…Precursor ion activation included injection of reagent ions, radical neutral species, photons, and electrons. Another recent work described an omnitrap-orbitrap platform equipped with infrared multiphoton dissociation, ultraviolet photodissociation, and electron capture dissociation for the analysis of peptides and proteins [88]. This new trend in commercial MS instrumentation is good news for research labs and industries, who can afford to purchase such systems.…”

Mass Spectrometry-Based Proteomics: Analyses Related to Drug-Resistance and Disease Biomarkers

“…Current literature suggests a new trend in MS/MS analysis of proteins/peptides, where multiple regimes of induced fragmentation are available within a single instrument. A recent work [53] described an instrument configuration based on the Orbitrap Explor is 480 mass spectrometer that has been coupled to an Omnitrap platform [54]. The Omnitrap possesses three distinct ion-activation regions that can be used to perform resonant-based collision-induced dissociation, several forms of electron-associated fragmentation, and Ultraviolet photodissociation.…”

Instrumentation at the Leading Edge of Proteomics

“…The combination of speed, sensitivity, and HR/AM led to quick adoption of the Q-Orbitrap platform across its various generations, as reflected in its leading use in proteomic research (Figure b). Additionally, several noncommercial modifications have enabled UVPD, − IRMPD, , SID, , and ECD , on Q-Orbitrap systems, and the newly developed Omnitrap brought multiple ion activation modes to Q-Orbitrap instruments. − …”