ArticleAnalytical chemistry2024
Simultaneous Native Mass Spectrometry Analysis of Single and Double Mutants To Probe Lipid Binding to Membrane Proteins.
Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Emerging roles of lipids in the flavivirus life cycle.Trends in microbiology · 2026Review
- Hybrid Detergents Facilitate Scalable Charge Reduction and Stabilize Membrane Proteins While Retaining Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- ZnJournal of the American Chemical Society · 2025Article
- Reduced Pressure Ionization Enhances Native Mass Spectrometry of Proteins and Protein Complexes.Angewandte Chemie (International ed. in English) · 2025Article
- Native Top-Down Analysis of Membrane Protein Complexes Directly From In Vitro and Native Membranes.Molecular & cellular proteomics : MCP · 2025Article
- Alanine Scanning to Define Membrane Protein-Lipid Interaction Sites Using Native Mass Spectrometry.Biochemistry · 2025Article
- Grafting the ALFA tag for structural studies of aquaporin Z.Journal of structural biology: X · 2024Article
- Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions.eLife · 2024Article
- Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
4 authors.
Funding
Abstract
Lipids are critical modulators of membrane protein structure and function. However, it is challenging to investigate the thermodynamics of protein-lipid interactions because lipids can simultaneously bind membrane proteins at different sites with different specificities. Here, we developed a native mass spectrometry (MS) approach using single and double mutants to measure the relative energetic contributions of specific residues on Aquaporin Z (AqpZ) toward cardiolipin (CL) binding. We first mutated potential lipid-binding residues on AqpZ, and mixed mutant and wild-type proteins together with CL. By using native MS to simultaneously resolve lipid binding to the mutant and wild-type proteins in a single spectrum, we directly determined the relative affinities of CL binding, thereby revealing the relative Gibbs free energy change for lipid binding caused by the mutation. Comparing different mutants revealed that W14 contributes to the tightest CL binding site, with R224 contributing to a lower affinity site. Using double mutant cycling, we investigated the synergy between W14 and R224 sites on CL binding. Overall, this novel native MS approach provides unique insights into the binding of lipids to specific sites on membrane proteins.
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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.