Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry
Synthetic peptides are a critical requirement for the development and application of targeted mass spectrometry (MS)-based assays for the quantitation of proteins from biological matrices. Transporting synthetic peptides on dry ice from one laboratory to another is costly and often difficult because...
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Online Access: | https://hdl.handle.net/1887/3250586 https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00249 https://doi.org/10.1021/acs.jproteome.1c00249 |
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ftunivleiden:oai:scholarlypublications.universiteitleiden.nl:item_3250586 2024-06-02T08:09:03+00:00 Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry Gaither, C. Popp, R. Borchers, S.P. Skarphedinsson, K. Eiriksson, F.F. Thorsteinsdottir, M. Mohammed, Y. Borchers, C.H. 2021 application/pdf https://hdl.handle.net/1887/3250586 https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00249 https://doi.org/10.1021/acs.jproteome.1c00249 en eng https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00249 doi:10.1021/acs.jproteome.1c00249 lumc-id: 122305759 https://hdl.handle.net/1887/3250586 Journal of Proteome Research multiple reaction monitoring (MRM) mass spectrometry peptide stability proteomics targeted proteomics internal standards Article / Letter to editor info:eu-repo/semantics/article Text 2021 ftunivleiden https://doi.org/10.1021/acs.jproteome.1c00249 2024-05-06T13:18:25Z Synthetic peptides are a critical requirement for the development and application of targeted mass spectrometry (MS)-based assays for the quantitation of proteins from biological matrices. Transporting synthetic peptides on dry ice from one laboratory to another is costly and often difficult because of country-specific import and export regulations. Therefore, in this study, we assessed the impact of leaving a lyophilized mixture consisting of 125 peptides at room temperature for up to 20 days, and we assessed the effect on the quantitative performance of multiple reaction monitoring-MS (MRM-MS) assays. The findings suggest that there are no significant differences in the MRM-MS results for the time points assessed in this study (up to 20 days). All the calibration curves and quality control (QC) samples met the acceptance criteria for precision and accuracy (raw data are available via the public MS data repository PanoramaWeb, identifier: /MRM Proteomics/2020_BAK125_RT). The number of endogenous proteins quantifiable across five plasma samples was consistently between 87 and 99 out of 125 for all time points. Moreover, the coefficients of variation (CVs) calculated for the majority of peptide concentrations across all samples and time points were <5%. In addition, a lyophilized peptide mixture was transported from Canada to Iceland without dry ice. The results showed that there was no significant difference in the quantitative performance, with the determined concentrations of most proteins in the samples falling within 30% between the analyses performed on the same three plasma samples in Iceland and those in Canada. Overall, a comparison of the results obtained in Canada and in Iceland indicated that the peptides were stable under the conditions tested and also indicated that shipping lyophilized peptide mixtures without dry ice, but in the presence of sufficient desiccant material, could be a feasible option in cases where transport difficulties may arise or dry-ice sublimation may occur. Proteomics Article in Journal/Newspaper Iceland Leiden University Scholarly Publications Canada Journal of Proteome Research 20 9 4292 4302 |
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Open Polar |
collection |
Leiden University Scholarly Publications |
op_collection_id |
ftunivleiden |
language |
English |
topic |
multiple reaction monitoring (MRM) mass spectrometry peptide stability proteomics targeted proteomics internal standards |
spellingShingle |
multiple reaction monitoring (MRM) mass spectrometry peptide stability proteomics targeted proteomics internal standards Gaither, C. Popp, R. Borchers, S.P. Skarphedinsson, K. Eiriksson, F.F. Thorsteinsdottir, M. Mohammed, Y. Borchers, C.H. Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
topic_facet |
multiple reaction monitoring (MRM) mass spectrometry peptide stability proteomics targeted proteomics internal standards |
description |
Synthetic peptides are a critical requirement for the development and application of targeted mass spectrometry (MS)-based assays for the quantitation of proteins from biological matrices. Transporting synthetic peptides on dry ice from one laboratory to another is costly and often difficult because of country-specific import and export regulations. Therefore, in this study, we assessed the impact of leaving a lyophilized mixture consisting of 125 peptides at room temperature for up to 20 days, and we assessed the effect on the quantitative performance of multiple reaction monitoring-MS (MRM-MS) assays. The findings suggest that there are no significant differences in the MRM-MS results for the time points assessed in this study (up to 20 days). All the calibration curves and quality control (QC) samples met the acceptance criteria for precision and accuracy (raw data are available via the public MS data repository PanoramaWeb, identifier: /MRM Proteomics/2020_BAK125_RT). The number of endogenous proteins quantifiable across five plasma samples was consistently between 87 and 99 out of 125 for all time points. Moreover, the coefficients of variation (CVs) calculated for the majority of peptide concentrations across all samples and time points were <5%. In addition, a lyophilized peptide mixture was transported from Canada to Iceland without dry ice. The results showed that there was no significant difference in the quantitative performance, with the determined concentrations of most proteins in the samples falling within 30% between the analyses performed on the same three plasma samples in Iceland and those in Canada. Overall, a comparison of the results obtained in Canada and in Iceland indicated that the peptides were stable under the conditions tested and also indicated that shipping lyophilized peptide mixtures without dry ice, but in the presence of sufficient desiccant material, could be a feasible option in cases where transport difficulties may arise or dry-ice sublimation may occur. Proteomics |
format |
Article in Journal/Newspaper |
author |
Gaither, C. Popp, R. Borchers, S.P. Skarphedinsson, K. Eiriksson, F.F. Thorsteinsdottir, M. Mohammed, Y. Borchers, C.H. |
author_facet |
Gaither, C. Popp, R. Borchers, S.P. Skarphedinsson, K. Eiriksson, F.F. Thorsteinsdottir, M. Mohammed, Y. Borchers, C.H. |
author_sort |
Gaither, C. |
title |
Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
title_short |
Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
title_full |
Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
title_fullStr |
Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
title_full_unstemmed |
Performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
title_sort |
performance assessment of a 125 human plasma peptide mixture stored at room temperature for multiple reaction monitoring-mass spectrometry |
publishDate |
2021 |
url |
https://hdl.handle.net/1887/3250586 https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00249 https://doi.org/10.1021/acs.jproteome.1c00249 |
geographic |
Canada |
geographic_facet |
Canada |
genre |
Iceland |
genre_facet |
Iceland |
op_source |
Journal of Proteome Research |
op_relation |
https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.1c00249 doi:10.1021/acs.jproteome.1c00249 lumc-id: 122305759 https://hdl.handle.net/1887/3250586 |
op_doi |
https://doi.org/10.1021/acs.jproteome.1c00249 |
container_title |
Journal of Proteome Research |
container_volume |
20 |
container_issue |
9 |
container_start_page |
4292 |
op_container_end_page |
4302 |
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1800754650892206080 |