ArticleJournal of the American Chemical Society2024
Detergents with Scalable Properties Identify Noncanonical Lipopolysaccharide Binding to Bacterial Inner Membrane Proteins.
Article in Journal of the American Chemical Society, 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, 9 citations in OpenAlex.
- Native Mass Spectrometry of Soluble Proteins with Sodium Chloride Enabled by a Dendritic Detergent.ACS measurement science au · 2026Article
- Hybrid Detergents Facilitate Scalable Charge Reduction and Stabilize Membrane Proteins While Retaining Lipid Interactions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Structural snapshots of Pseudomonas aeruginosa LptBNature communications · 2025Article
- Drop Dilution Enables the Use of PEG-Derived Detergents for Membrane Protein Purification.ACS omega · 2025Article
- Expanding the Reach of Membrane Protein-Ligand Interaction Studies Through the Integration of Mass Spectrometry and Membrane Mimetics.Proteomics · 2025Review
- Deep Structural Characterization of Protein-Bound Lipids via Native MS and Ultraviolet Photodissociation.Analytical chemistry · 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
- Chemical linkers switch triglycerol detergents from bacterial protein purification to mild antibiotic amplification.Communications chemistry · 2025Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopolysaccharide (LPS) is vital for maintaining the outer membrane barrier in Gram-negative bacteria. LPS is also frequently obtained in complex with the inner membrane proteins after detergent purification. The question of whether or not LPS binding to inner membrane proteins not involved in outer membrane biogenesis reflects native lipid environments remains unclear. Here, we leverage the control of the hydrophilic-lipophilic balance and packing parameter concepts to chemically tune detergents that can be used to qualitatively differentiate the degree to which proteins copurify with phospholipids (PLs) and/or LPS. Given the scalable properties of these detergents, we demonstrate a detergent fine-tuning that enables the facile investigation of intact proteins and their complexes with lipids by native mass spectrometry (nMS). We conclude that LPS, a lipid that is believed to be important for outer membranes, can also affect the activity of membrane proteins that are currently not assigned to be involved in outer membrane biogenesis. Our results deliver a scalable detergent chemistry for a streamlined biophysical characterization of protein-lipid interactions, provide a rationale for the high affinity of LPS-protein binding, and identify noncanonical associations between LPS and inner membrane proteins with relevance for membrane biology and antibiotic research.
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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 OpenQuestion graph.