ArticleJournal of biomolecular NMR2001
Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR.
Article in Journal of biomolecular NMR, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 120 citations in OpenAlex.
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- Probing and Manipulating the Lateral Pressure Profile in Lipid Bilayers Using Membrane-Active Peptides-A Solid-StateInternational journal of molecular sciences · 2022Article
- Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-DrivenThe journal of physical chemistry. B · 2018Article
- Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei.Amino acids · 2018Article
- Therapeutic Potential of Gramicidin S in the Treatment of Root Canal Infections.Pharmaceuticals (Basel, Switzerland) · 2016Article
- Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides.Frontiers in cell and developmental biology · 2016Article
- Synergistic effect of membrane-active peptides polymyxin B and gramicidin S on multidrug-resistant strains and biofilms of Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2015Article
- Fermentation and Cost-Effective 13C/15N Labeling of the Nonribosomal Peptide Gramicidin S for Nuclear Magnetic Resonance Structure Analysis.Applied and environmental microbiology · 2015Article
- 3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.Biophysical journal · 2014Article
- The high resolution structure of tyrocidine A reveals an amphipathic dimer.Biochimica et biophysica acta · 2014Article
- Specific fluorine labeling of the HyHEL10 antibody affects antigen binding and dynamics.Biochemistry · 2012Article
- Determining the orientation and localization of membrane-bound peptides.Current protein & peptide science · 2012Review
- Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.European biophysics journal : EBJ · 2011Article
- Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.Biochimica et biophysica acta · 2011Article
- Gramicidin S and polymyxins: the revival of cationic cyclic peptide antibiotics.Cellular and molecular life sciences : CMLS · 2009Review
- Synergistic interaction between silver nanoparticles and membrane-permeabilizing antimicrobial peptides.Antimicrobial agents and chemotherapy · 2009Article
- Influence of whole-body dynamics on 15N PISEMA NMR spectra of membrane proteins: a theoretical analysis.Biophysical journal · 2009Article
- Orientation and dynamics of peptides in membranes calculated from 2H-NMR data.Biophysical journal · 2009Article
- Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides.Journal of medicinal chemistry · 2009Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antimicrobial properties of the cyclic beta-sheet peptide gramicidin S are attributed to its destabilizing effect on lipid membranes. Here we present the membrane-bound structure and alignment of a derivative of this peptide, based on angular and distance constraints. Solid-state 19F-NMR was used to study a 19F-labelled gramicidin S analogue in dimyristoylphosphatidylcholine bilayers at a lipid:peptide ratio of 80:1 and above. Two equivalent leucine side chains were replaced by the non-natural amino acid 4F-phenylglycine, which serves as a highly sensitive reporter on the structure and dynamics of the peptide backbone. Using a modified CPMG multipulse sequence, the distance between the two 19F-labels was measured from their homonuclear dipolar coupling as 6 A. in good agreement with the known backbone structure of natural gramicidin S in solution. By analyzing the anisotropic chemical shift of the 19F-labels in macroscopically oriented membrane samples, we determined the alignment of the peptide in the bilayer and described its temperature-dependent mobility. In the gel phase, the 19F-labelled gramicidin S is aligned symmetrically with respect to the membrane normal, i.e., with its cyclic beta-sheet backbone lying flat in the plane of the bilayer, which is fully consistent with its amphiphilic character. Upon raising the temperature to the liquid crystalline state, a considerable narrowing of the 19F-NMR chemical shift dispersion is observed, which is attributed the onset of global rotation of the peptide and further wobbling motions. This study demonstrates the potential of the 19F nucleus to describe suitably labelled polypeptides in membranes, requiring only little material and short NMR acquisition times.
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