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Concentration‐dependent coulombic effects in travelling wave ion mobility spectrometry collision cross section calibration

Eldrid, C; O'Connor, E; Thalassinos, K; (2020) Concentration‐dependent coulombic effects in travelling wave ion mobility spectrometry collision cross section calibration. Rapid Communications in Mass Spectrometry , 34 (S4) , Article e8613. 10.1002/rcm.8613. Green open access

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Abstract

RATIONALE: Travelling wave ion mobility spectrometry (TWIMS) is increasingly being used as a method for calculating the collision cross section (CCS) of protein ions. To calculate the CCS of unknown ions, however, the TWIMS device needs to be calibrated using calibrant proteins of known CCS values. The effect of calibrant protein concentration of the accuracy of the resulting calibration curve has not been explicitly studied so far. We hypothesised that at high protein concentrations the ion density within the TWIMS device will be such that ions will experience space charge effects resulting in deviations, as well as broadening, of ion arrival time distributions (ATDs). Calibration curves using these altered ATDs would therefore result in incorrect CCS values being calculated for the protein ions of interest. // METHODS: Three protein CCS calibrants, avidin, bovine serum albumin and β-lactgobulin, were prepared at different concentrations and used to calculate the CCS of a non-calibrant protein. Data were collected on a Synapt G1 ion mobility-mass spectrometer with a nano-electrospray ionisation (nESI) source using capillaries prepared in house. // RESULTS: Increasing the concentration of CCS calibrants caused ATD broadening and shifted the ATD peak tops, leading to a significant increase in calculated CCS values. // CONCLUSION: The concentration of protein calibrants can directly affect the quality of the CCS calibration in TWIMS experiments.

Type: Article
Title: Concentration‐dependent coulombic effects in travelling wave ion mobility spectrometry collision cross section calibration
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/rcm.8613
Publisher version: https://doi.org/10.1002/rcm.8613
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10085286
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