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Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation: Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios

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Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation : Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios. / Simpson, Joanna P.; Fascione, Martin; Bergström, Ed; Wilson, Julie; Collins, Matthew J.; Penkman, Kirsty E.H.; Thomas-Oates, Jane.

In: Rapid Communications in Mass Spectrometry, Vol. 33, No. 12, 30.06.2019, p. 1049-1057.

Research output: Contribution to journalArticle

Harvard

Simpson, JP, Fascione, M, Bergström, E, Wilson, J, Collins, MJ, Penkman, KEH & Thomas-Oates, J 2019, 'Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation: Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios', Rapid Communications in Mass Spectrometry, vol. 33, no. 12, pp. 1049-1057. https://doi.org/10.1002/rcm.8441

APA

Simpson, J. P., Fascione, M., Bergström, E., Wilson, J., Collins, M. J., Penkman, K. E. H., & Thomas-Oates, J. (2019). Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation: Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios. Rapid Communications in Mass Spectrometry, 33(12), 1049-1057. https://doi.org/10.1002/rcm.8441

Vancouver

Simpson JP, Fascione M, Bergström E, Wilson J, Collins MJ, Penkman KEH et al. Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation: Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios. Rapid Communications in Mass Spectrometry. 2019 Jun 30;33(12):1049-1057. https://doi.org/10.1002/rcm.8441

Author

Simpson, Joanna P. ; Fascione, Martin ; Bergström, Ed ; Wilson, Julie ; Collins, Matthew J. ; Penkman, Kirsty E.H. ; Thomas-Oates, Jane. / Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation : Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios. In: Rapid Communications in Mass Spectrometry. 2019 ; Vol. 33, No. 12. pp. 1049-1057.

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@article{d0fd5faef70e4ca18f74f67d947c7855,
title = "Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation: Synthetic peptide studies demonstrate electrospray ionisation gives more reliable response ratios",
abstract = "RATIONALE: Although mass spectrometry is routinely used to determine deamination in peptide mixtures, the effects of ionisation source choice have not yet been investigated. In particular, matrix-assisted laser desorption/ionisation (MALDI) has become a popular tool with which to measure levels of glutamine deamidation in ancient proteins. Here we use model synthetic peptides to rigorously compare MALDI and electrospray ionisation. METHODS: We use two synthetic peptides, with glutamine (Q) in one substituted for glutamic acid (E) in the other, to investigate the suitability of MALDI and ESI sources for the assessment of deamidation in peptides using mass spectrometry. We also compare measurements of the same Q and E-containing peptide mixtures using two different mass analysers (time of flight and Fourier-transform ion cyclotron resonance).RESULTS: When standard mixtures of the Q- and E-containing peptides were analysed using MALDI, under-representation of the E-containing peptide was observed. This observation was consistent between analyses carried out using either TOF or FT-ICR-MS. When the same mixtures were analysed using ESI FT-ICR-MS, no ionisation bias was observed. CONCLUSIONS: MALDI may not be a suitable ionisation method for the determination of deamidation in peptide mixtures. However, ESI was successfully used to determine the ratio in known mixtures of Q and E containing peptides. These preliminary observations warrant further investigation into ionisation bias when measuring deamidation in other peptide sequences.",
author = "Simpson, {Joanna P.} and Martin Fascione and Ed Bergstr{\"o}m and Julie Wilson and Collins, {Matthew J.} and Penkman, {Kirsty E.H.} and Jane Thomas-Oates",
note = "{\circledC} 2019 The Authors",
year = "2019",
month = "6",
day = "30",
doi = "10.1002/rcm.8441",
language = "English",
volume = "33",
pages = "1049--1057",
journal = "Rapid communications in mass spectrometry",
issn = "0951-4198",
publisher = "John Wiley and Sons Ltd",
number = "12",

}

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TY - JOUR

T1 - Ionisation bias undermines the use of matrix-assisted laser desorption/ionisation for estimating peptide deamidation

T2 - Rapid communications in mass spectrometry

AU - Simpson, Joanna P.

AU - Fascione, Martin

AU - Bergström, Ed

AU - Wilson, Julie

AU - Collins, Matthew J.

AU - Penkman, Kirsty E.H.

AU - Thomas-Oates, Jane

N1 - © 2019 The Authors

PY - 2019/6/30

Y1 - 2019/6/30

N2 - RATIONALE: Although mass spectrometry is routinely used to determine deamination in peptide mixtures, the effects of ionisation source choice have not yet been investigated. In particular, matrix-assisted laser desorption/ionisation (MALDI) has become a popular tool with which to measure levels of glutamine deamidation in ancient proteins. Here we use model synthetic peptides to rigorously compare MALDI and electrospray ionisation. METHODS: We use two synthetic peptides, with glutamine (Q) in one substituted for glutamic acid (E) in the other, to investigate the suitability of MALDI and ESI sources for the assessment of deamidation in peptides using mass spectrometry. We also compare measurements of the same Q and E-containing peptide mixtures using two different mass analysers (time of flight and Fourier-transform ion cyclotron resonance).RESULTS: When standard mixtures of the Q- and E-containing peptides were analysed using MALDI, under-representation of the E-containing peptide was observed. This observation was consistent between analyses carried out using either TOF or FT-ICR-MS. When the same mixtures were analysed using ESI FT-ICR-MS, no ionisation bias was observed. CONCLUSIONS: MALDI may not be a suitable ionisation method for the determination of deamidation in peptide mixtures. However, ESI was successfully used to determine the ratio in known mixtures of Q and E containing peptides. These preliminary observations warrant further investigation into ionisation bias when measuring deamidation in other peptide sequences.

AB - RATIONALE: Although mass spectrometry is routinely used to determine deamination in peptide mixtures, the effects of ionisation source choice have not yet been investigated. In particular, matrix-assisted laser desorption/ionisation (MALDI) has become a popular tool with which to measure levels of glutamine deamidation in ancient proteins. Here we use model synthetic peptides to rigorously compare MALDI and electrospray ionisation. METHODS: We use two synthetic peptides, with glutamine (Q) in one substituted for glutamic acid (E) in the other, to investigate the suitability of MALDI and ESI sources for the assessment of deamidation in peptides using mass spectrometry. We also compare measurements of the same Q and E-containing peptide mixtures using two different mass analysers (time of flight and Fourier-transform ion cyclotron resonance).RESULTS: When standard mixtures of the Q- and E-containing peptides were analysed using MALDI, under-representation of the E-containing peptide was observed. This observation was consistent between analyses carried out using either TOF or FT-ICR-MS. When the same mixtures were analysed using ESI FT-ICR-MS, no ionisation bias was observed. CONCLUSIONS: MALDI may not be a suitable ionisation method for the determination of deamidation in peptide mixtures. However, ESI was successfully used to determine the ratio in known mixtures of Q and E containing peptides. These preliminary observations warrant further investigation into ionisation bias when measuring deamidation in other peptide sequences.

UR - http://www.scopus.com/inward/record.url?scp=85066498192&partnerID=8YFLogxK

U2 - 10.1002/rcm.8441

DO - 10.1002/rcm.8441

M3 - Article

VL - 33

SP - 1049

EP - 1057

JO - Rapid communications in mass spectrometry

JF - Rapid communications in mass spectrometry

SN - 0951-4198

IS - 12

ER -