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Updated: Apr 17, 2026
Determination of the Gas-phase Acidities of Oligopeptides
Published on: June 24, 2013
Matrix effect explained by unexpected formation of peptide in acidified plasma
Martin Ahnoff1, Ann-Christin Nyström, Fritz Schweikart
1Department of Chemistry & Molecular Biology, University of Gothenburg, SE-412 96 Gothenburg, Sweden.
Aim:
Peak distortion and strong signal enhancement was observed when applying a bioanalytical method based on mixed-mode SPE, hydrophilic interaction chromatography and ESI-MS to acidified rabbit plasma samples.
Results:
High-resolution ESI-MS and N-terminal peptide sequencing revealed a peptide NFQNAL, which was confirmed by H/D exchange ESI-MS.
Conclusion:
The peptide causing the observed matrix effect was formed by enzymatic degradation of serum albumin at pH 3. Degradation required both acidification and presence of other plasma constituents in addition to albumin to take place. The degree of signal enhancement correlated to the level of NFQNAL in the ion source as measured by MS, with a maximal enhancement factor of 3 at intermediate levels of NFQNAL. The interference was eliminated by changing to another type of hydrophilic interaction chromatography column.
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