ArticleAnalytical chemistry2025
Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Native mass spectrometry enabled by infrared matrix-assisted laser desorption electrospray ionization for rapid measurement of protein-ligand biophysical parameters.Analytical and bioanalytical chemistry · 2026Article
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5 authors.
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Abstract
Native mass spectrometry (nMS) is routinely used to monitor ligand binding in protein complexes. However, such interactions are easily distorted by unwanted dissociation during desolvation and ionization. This effect can be mitigated by chemical additives that modulate the ion charge, which results in lower-energy ions and better-preserved interactions. While positive-mode is the most used ionization approach, the use of negative-mode ionization has attracted attention due to its surprising ability to reduce the dissociation of some protein complexes. We therefore investigated whether charge-reducing compounds that stabilize proteins in positive ionization mode, such as imidazole, acetonitrile, and trimethylammonium-
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