ArticleJournal of the American Chemical Society2008
Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating Peptide example.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Advances in molecular dynamics approaches for investigating cell-penetrating peptides.Biophysical reviews · 2026Review
- Unexpected asymmetric distribution of cholesterol and phospholipids in equilibrium model membranes.Biophysical journal · 2024Article
- Phospholipid Membrane Interactions of Model Ac-WL-X-LL-OH Peptides Investigated by Solid-State Nuclear Magnetic Resonance.Membranes · 2024Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes.Angewandte Chemie (International ed. in English) · 2022Article
- Peptide-based delivery of therapeutics in cancer treatment.Materials today. Bio · 2022Review
- Structure of membrane diacylglycerol kinase in lipid bilayers.Communications biology · 2021Article
- Dimer Organization of Membrane-Associated NS5A of Hepatitis C Virus as Determined by Highly SensitiveAngewandte Chemie (International ed. in English) · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Gadolinium Complexes as Contrast Agent for Cellular NMR Spectroscopy.International journal of molecular sciences · 2020Article
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- Cholesterol re-organisation and lipid de-packing by arginine-rich cell penetrating peptides: Role in membrane translocation.PloS one · 2019Article
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Determining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Journal of biomolecular NMR · 2013Article
- Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.Amino acids · 2013Review
- Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Journal of the American Chemical Society · 2012Article
- Membrane protein structure and dynamics from NMR spectroscopy.Annual review of physical chemistry · 2012Review
- Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR.Journal of biomolecular NMR · 2011Article
- Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen.Journal of biomolecular NMR · 2011Article
- Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Protein science : a publication of the Protein Society · 2011Article
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3 authors.
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Abstract
A novel solid-state NMR technique for identifying the asymmetric insertion depths of membrane proteins in lipid bilayers is introduced. By applying Mn (2+) ions on the outer but not the inner leaflet of lipid bilayers, the sidedness of protein residues in the lipid bilayer can be determined through paramagnetic relaxation enhancement (PRE) effects. Protein-free lipid membranes with one-side Mn (2+)-bound surfaces exhibit significant residual (31)P and lipid headgroup (13)C intensities, in contrast to two-side Mn (2+)-bound membranes, where lipid headgroup signals are mostly suppressed. Applying this method to a cell-penetrating peptide, penetratin, we found that at low peptide concentrations, penetratin is distributed in both leaflets of the bilayer, in contrast to the prediction of the electroporation model, which predicts that penetratin binds to only the outer lipid leaflet at low peptide concentrations to cause an electric field that drives subsequent peptide translocation. The invalidation of the electroporation model suggests an alternative mechanism for intracellular import of penetratin, which may involve guanidinium-phosphate complexation between the peptide and the lipids.
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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.