ArticleJournal of the American Society for Mass Spectrometry2021
Electrospray-Induced Mass Spectrometry Is Not Suitable for Determination of Peptidic Cu(II) Complexes.
Article in Journal of the American Society for Mass Spectrometry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Mild and efficient coupling reactions enabled byCatalysis science & technology · 2026Article
- Small Cysteine-Rich Motif, Big Function─Metal-Driven Dimerization of the CopY C-Terminal Fragment.Inorganic chemistry · 2025Article
- APP-C31: An Intracellular Promoter of Both Metal-Free and Metal-Bound Amyloid-βAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- From methodological limitations to the function of metallothioneins - a guide to approaches for determining weak, moderate, and tight affinity zinc sites.Metallomics : integrated biometal science · 2023Article
- Zn(II) to Ag(I) Swap in Rad50 Zinc Hook Domain Leads to Interprotein Complex Disruption through the Formation of Highly Stable AgInorganic chemistry · 2023Article
- Reactive Cu2+-peptide intermediates revealed by kinetic studies gain relevance by matching time windows in copper metallomics.Metallomics : integrated biometal science · 2023Article
- An Overlooked Hepcidin-Cadmium Connection.International journal of molecular sciences · 2022Article
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4 authors.
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Abstract
The toolset of mass spectrometry (MS) is still expanding, and the number of metal ion complexes researched this way is growing. The Cu(II) ion forms particularly strong peptide complexes of biological interest which are frequent objects of MS studies, but quantitative aspects of some reported results are at odds with those of experiments performed in solution. Cu(II) complexes are usually characterized by fast ligand exchange rates, despite their high affinity, and we speculated that such kinetic lability could be responsible for the observed discrepancies. In order to resolve this issue, we selected peptides belonging to the ATCUN family characterized with high and thoroughly determined Cu(II) binding constants and re-estimated them using two ESI-MS techniques: standard conditions in combination with serial dilution experiments and very mild conditions for competition experiments. The sample acidification, which accompanies the electrospray formation, was simulated with the pH-jump stopped-flow technique. Our results indicate that ESI-MS should not be used for quantitative studies of Cu(II)-peptide complexes because the electrospray formation process compromises the entropic contribution to the complex stability, yielding underestimations of complex stability constants.
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