ArticleNature communications2023
Polyamine detergents tailored for native mass spectrometry studies of membrane proteins.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- Probing the Annular Lipid Belt of Membrane Proteins Using Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Hybrid Detergents Facilitate Scalable Charge Reduction and Stabilize Membrane Proteins While Retaining Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Recent Advances in Detergent Chemistry and Handling Support Membrane Protein Analysis Including Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Review
- Design and Synthesis of Hetero-Bicephalic Detergents for Native Mass Spectrometry of Membrane Proteins.Journal of the American Chemical Society · 2025Article
- Native Mass Spectrometry of Membrane Protein-Lipid Interactions in Different Detergent Environments.Analytical chemistry · 2024Article
- Proteomic Investigation of Immune Checkpoints and Some of Their Inhibitors.International journal of molecular sciences · 2024Review
- Native mass spectrometry of membrane protein-lipid interactions in different detergent environments.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Native mass spectrometry (MS) is a powerful technique for interrogating membrane protein complexes and their interactions with other molecules. A key aspect of the technique is the ability to preserve native-like structures and noncovalent interactions, which can be challenging depending on the choice of detergent. Different strategies have been employed to reduce charge on protein complexes to minimize activation and preserve non-covalent interactions. Here, we report the synthesis of a class of polyamine detergents tailored for native MS studies of membrane proteins. These detergents, a series of spermine covalently attached to various alkyl tails, are exceptional charge-reducing molecules, exhibiting a ten-fold enhanced potency over spermine. Addition of polyamine detergents to proteins solubilized in maltoside detergents results in improved, charge-reduced native mass spectra and reduced dissociation of subunits. Polyamine detergents open new opportunities to investigate membrane proteins in different detergent environments that have thwarted previous native MS studies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.