Infrared Photoactivation Enables nano-DESI MS of Protein Complexes in Tissue on a Linear Ion Trap Mass Spectrometer DOI
Oliver J. Hale, Todd H. Mize, Helen J. Cooper

et al.

Journal of the American Society for Mass Spectrometry, Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 27, 2024

Native mass spectrometry analysis of proteins directly from tissues can be performed by using nanospray-desorption electrospray ionization (nano-DESI). Typically, supplementary collisional activation is essential to decluster protein complex ions solvent, salt, detergent, and lipid clusters that comprise the ion beam. As an alternative, we have implemented declustering infrared (IR) photoactivation on a linear trap spectrometer equipped with CO

Language: Английский

A Robust and Automated Platform for Charge Detection Mass Spectrometry of Megadalton Biotherapeutics DOI
Samuel E. Janisse, Ryan T. Fellers,

Shannon A. Raab

et al.

Analytical Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 19, 2025

Gene therapies based on adeno-associated viruses are an emerging area with high potential to improve human health. Current quality control techniques assess contaminates and byproducts from the virus (AAV) production pipelines lacking in robustness throughput. To address these limitations, we coupled automated microfluidic device called SampleStream Orbitrap-based charge detection mass spectrometry (SS-CDMS). We demonstrate that SS-CDMS workflow performs AAV analysis under 15 min per sample a completely autonomous manner. The enables rapid assessment of key attributes (CQAs), such as molecular weight content ratio formulations small requirement (<2 × 109 capsids) without being limited by concentration. Additionally, this work shows for be implemented at various stages pipeline through effective clean up more complex matrices cell culture media.

Language: Английский

Citations

0

Roughhousing with Ions: Surface-Induced Dissociation and Electron Capture Dissociation as Diagnostics of Q-Cyclic IMS-TOF Instrument Tuning Gentleness DOI
Andrew J. Arslanian, Vicki H. Wysocki

Journal of the American Society for Mass Spectrometry, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 7, 2024

Native mass spectrometry can characterize a range of biomolecular features pertinent to structural biology, including intact mass, stoichiometry, ligand-bound states, and topology. However, when an instrument's ionization source is tuned maximize signal intensity or adduct removal, it possible that the complex's tertiary quaternary structures be rearranged in way no longer reflect its native-like conformation. This could affect downstream ion activation experiments, leading erroneous conclusions about structure. One strategy surface-induced dissociation (SID), which generally causes protein complexes dissociate along weakest subunit interfaces, revealing critical information topology connectivity. If structure has been disturbed, then SID fingerprint will shift as well. Thus, was used diagnose source-induced rearrangement help tune other upstream transmission regions strike balance between intensity, conserving Complementary SID, electron-capture (ECD) also after in-source confirm interfaces were rearranged, opening electron capture subsequent dissociation. These results provide valuable guide for new practitioners native highlight importance using standard tuning instrument platforms optimal performance.

Language: Английский

Citations

2

Infrared photoactivation enables nano-DESI MS of protein complexes from tissue on a linear ion trap mass spectrometer. DOI Creative Commons
Oliver J. Hale, Todd H. Mize, Helen J. Cooper

et al.

Published: Aug. 9, 2024

Native mass spectrometry analysis of proteins directly from tissues can be performed using nanospray-desorption electrospray ionization (nano-DESI). Typically, supplementary collisional activation is essential to decluster protein complex ions solvent, salt, detergent and lipid clusters that comprise the ion beam. As an alternative, we have implemented declustering by infrared (IR) photoactivation on a linear trap spectrometer equipped with CO2 laser. The prototype system demonstrates intact up approx. 50 kDa in molecular weight were sampled brain eye lens nano-DESI. For example, signals attributable different metal binding states hSOD1G93A homodimers (approx. 32 kDa) separated only 6 Th (10+ ions) resolved IR declustering, but not activation. We found outperform its ability reduce chemical background non-specific nano-DESI also situ native MS low-cost potential spectrometers for this type analysis.

Language: Английский

Citations

1

Infrared Photoactivation Enables nano-DESI MS of Protein Complexes in Tissue on a Linear Ion Trap Mass Spectrometer DOI
Oliver J. Hale, Todd H. Mize, Helen J. Cooper

et al.

Journal of the American Society for Mass Spectrometry, Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 27, 2024

Native mass spectrometry analysis of proteins directly from tissues can be performed by using nanospray-desorption electrospray ionization (nano-DESI). Typically, supplementary collisional activation is essential to decluster protein complex ions solvent, salt, detergent, and lipid clusters that comprise the ion beam. As an alternative, we have implemented declustering infrared (IR) photoactivation on a linear trap spectrometer equipped with CO

Language: Английский

Citations

1