Regarding Emitter Positioning for Nanoflow Electrospray Ionization

Nanoflow electrospray ionization is commonly used for proteomics due to its high sensitivity. Signal intensity, however, is dependent on optimal emitter positioning relative to the mass spectrometer inlet. Here, we characterize the effect of varied emitter positions on peptide signal intensity in all three dimensions using emitters and flows consistent with standard proteomic analyses. We observe improved signal robustness to x/y variations at increasing z distances and demonstrate that positioning within 1 to 2 mm of the optimal location will maintain consistent signal. Signal intensity behavior is consistent across the m/z range, suggesting a certain level of analyte-independence for proteomics analyses. These results provide insight for proteomics researchers using nanoflow LC-MS/MS.

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Publication Details

Journal
bioRxiv (Cold Spring Harbor Laboratory)
Published
2025-12-20
DOI
https://doi.org/10.64898/2025.12.18.695161
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
Field-Weighted Citation Impact
0.00

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article

Regarding Emitter Positioning for Nanoflow Electrospray Ionization

bioRxiv (Cold Spring Harbor Laboratory)
Mass Spectrometry Techniques and Applications
article

Regarding Emitter Positioning for Nanoflow Electrospray Ionization

article en

Abstract

Nanoflow electrospray ionization is commonly used for proteomics due to its high sensitivity. Signal intensity, however, is dependent on optimal emitter positioning relative to the mass spectrometer inlet. Here, we characterize the effect of varied emitter positions on peptide signal intensity in all three dimensions using emitters and flows consistent with standard proteomic analyses. We observe improved signal robustness to x/y variations at increasing z distances and demonstrate that positioning within 1 to 2 mm of the optimal location will maintain consistent signal. Signal intensity behavior is consistent across the m/z range, suggesting a certain level of analyte-independence for proteomics analyses. These results provide insight for proteomics researchers using nanoflow LC-MS/MS.

bioRxiv (Cold Spring Harbor Laboratory)
University of Wisconsin–Madison (US), Morgridge Institute for Research (US)
National Institutes of Health
Openalex Percentile: Top 63%
Mass Spectrometry Techniques and Applications
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