Cited by 20Advanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and ApplicationsMicrofluidic and Capillary Electrophoresis Applications

Optimization of mass spectrometric parameters improve the identification performance of capillary zone electrophoresis for single-shot bottom-up proteomics analysis

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Zhang, Zhenbin, Dovichi, Norman J.·2018·Analytica Chimica Acta

Abstract

The effects of MS1 injection time, MS2 injection time, dynamic exclusion time, intensity threshold, and isolation width were investigated on the numbers of peptide and protein identifications for single-shot bottom-up proteomics analysis using CZE-MS/MS analysis of a Xenopus laevis tryptic digest. An electrokinetically pumped nanospray interface was used to couple a linear-polyacrylamide coated capillary to a Q Exactive HF mass spectrometer. A sensitive method that used a 1.4 Th isolation width, 60,000 MS2 resolution, 110 ms MS2 injection time, and a top 7 fragmentation produced the largest number of identifications when the CZE loading amount was less than 100 ng. A programmable autogain control method (pAGC) that used a 1.4 Th isolation width, 15,000 MS2 resolution, 110 ms MS2 injection time, and top 10 fragmentation produced the largest number of identifications for CZE loading amounts greater than 100 ng; 7218 unique peptides and 1653 protein groups were identified from 200 ng by using the pAGC method. The effect of mass spectrometer conditions on the performance of UPLC-MS/MS was also investigated. A fast method that used a 1.4 Th isolation width, 30,000 MS2 resolution, 45 ms MS2 injection time, and top 12 fragmentation produced the largest number of identifications for 200 ng UPLC loading amount (6025 unique peptides and 1501 protein groups). This is the first report where the identification number for CZE surpasses that of the UPLC at the 200 ng loading level. However, more peptides (11476) and protein groups (2378) were identified by using UPLC-MS/MS when the sample loading amount was increased to 2 μg with the fast method. To exploit the fast scan speed of the Q-Exactive HF mass spectrometer, higher sample loading amounts are required for single-shot bottom-up proteomics analysis using CZE-MS/MS.

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Crossref · 10.1016/j.aca.2017.11.023

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  • CZE has proven valuable for protein identification via bottom-up proteomics, where ultrasensitive and fast analysis can be obtained.

    “CZE has also proven to be a valuable tool for protein identification via bottom-up proteomics where ultrasensitive and fast analysis can be obtained72–74.”

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References 25 · Cited by 20

Authors
Zhang, Z., & Dovichi, N. J.
Affiliations
University of Notre Dame (US)
Venue
Analytica Chimica Acta
Publisher
Elsevier BV
Published
2018-02
Volume
1001
Pages
93-99
ISSN
0003-2670 (ISSN-L)
OpenAlex
W2769584918
Cited by
20
References
25
Citations by year
2025: 3 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 5 · 2018: 6
FWCI
1.62
Type
journal article
Language
en
Open access
Locations
  • Analytica Chimica Acta (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institutes of Health (R01GM096767)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
  • Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
Keywords
capillary zone electrophoresis, shotgun proteomics, intensity threshold, peptide identification, protein identification, Xenopus laevis, tryptic digest
MeSH terms
Animals, Peptides, Xenopus laevis, Electrophoresis, Capillary, Spectrometry, Mass, Electrospray Ionization, Xenopus Proteins, Proteomics, Tandem Mass Spectrometry

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