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Related Experiment Videos

Nanospray 'taxation' and how to avoid it.

I V Chernushevich1, U Bahr, M Karas

  • 1MDS SCIEX, 71 Four Valley Drive, Concord, L4K 4V8 Canada.

Rapid Communications in Mass Spectrometry : RCM
|September 24, 2004
PubMed
Summary

Analyte loss in nanospray ionization mass spectrometry is linked to glass capillary surface charge, affecting peptides with positive charges. This impacts protein analysis, especially for mutations and modifications.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Mass Spectrometry

Background:

  • Nanospray ionization (NSI) is a crucial technique in mass spectrometry.
  • Analyte loss and delayed detection have been observed in NSI, impacting data reliability.
  • The cause of these losses, particularly concerning charged analytes, requires further investigation.

Purpose of the Study:

  • To investigate the cause of analyte loss and delayed detection in NSI mass spectrometry.
  • To understand the role of the capillary surface charge in analyte interactions.
  • To assess the impact of these losses on protein identification and characterization.

Main Methods:

  • Mass spectrometric analysis using nanospray ionization with glass and quartz capillaries.
  • Cation-exchange chromatography principles applied to understand surface interactions.
  • Analysis of peptide mixtures and bovine serum albumin (BSA) tryptic digests at sub-micromolar concentrations.

Main Results:

  • Analyte loss and delayed detection were correlated with the negative charge on glass nanospray capillary surfaces.
  • Peptides and proteins with localized positive charges, particularly blocks of basic amino acids, showed higher affinity for the glass surface.
  • Approximately 20% fewer tryptic peptides were identified using glass capillaries compared to quartz or conventional electrospray.

Conclusions:

  • The negative surface charge of glass nanospray capillaries causes cation-exchange interactions, leading to analyte loss.
  • This phenomenon primarily affects peptides and proteins with localized positive charges.
  • While general protein identification may be unaffected, detailed analyses like mutation or PTM studies could suffer from reduced sequence coverage.

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