ArticleBiophysical journal1999
Orientation of cecropin A helices in phospholipid bilayers determined by solid-state NMR spectroscopy.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Beyond static pores: A dynamic mechanism of antimicrobial action.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural pores not required: Antimicrobial peptides induce ion permeabilization of lipid membranes through transient water channels.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- OMN6 a novel bioengineered peptide for the treatment of multidrug resistant Gram negative bacteria.Scientific reports · 2021Article
- Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pestThe journal of venomous animals and toxins including tropical diseases · 2021Article
- De novo Design of Selective Membrane-Active Peptides by Enzymatic Control of Their Conformational Bias on the Cell Surface.Angewandte Chemie (International ed. in English) · 2019Article
- Novel Hybrid Peptide Cecropin A (1-8)-LL37 (17-30) with Potential Antibacterial Activity.International journal of molecular sciences · 2016Article
- Functional Roles of Aromatic Residues and Helices of Papiliocin in its Antimicrobial and Anti-inflammatory Activities.Scientific reports · 2015Article
- Localized permeabilization of E. coli membranes by the antimicrobial peptide Cecropin A.Biochemistry · 2013Article
- Antimicrobial peptides and induced membrane curvature: geometry, coordination chemistry, and molecular engineering.Current opinion in solid state & materials science · 2013Article
- A common landscape for membrane-active peptides.Protein science : a publication of the Protein Society · 2013Review
- The discreet charm of the curve.Biophysical journal · 2013Article
- Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus.The Journal of biological chemistry · 2011Article
- Antimicrobial peptides: modes of mechanism, modulation of defense responses.Plant signaling & behavior · 2011Review
- Crystallization and preliminary X-ray analysis of cecropin B from Bombyx mori.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies.Biophysical journal · 2010Article
- Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Biochemistry · 2009Article
- A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A.Biophysical journal · 2008Article
- Antimicrobial peptide-lipid binding interactions and binding selectivity.Biophysical journal · 2007Article
- Mechanism of the cell-penetrating peptide transportan 10 permeation of lipid bilayers.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The orientation of the insect antibiotic peptide cecropin A (CecA) in the phospholipid bilayer membrane was determined using (15)N solid-state NMR spectroscopy. Two peptide samples, each specifically labeled with (15)N at Val(11) or Ala(27), were synthesized by solid phase techniques. The peptides were incorporated into phospholipid bilayers, prepared from a mixture of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol, and oriented on glass slides. The (15)N chemical shift solid-state NMR spectra from these uniaxially oriented samples display a single (15)N chemical shift frequency for each labeled residue. Both frequencies are near the upfield end of the (15)N chemical shift powder pattern, as expected for an alpha-helix with its long axis in the plane of the membrane and the NH bonds perpendicular to the direction of the magnetic field. These results support a mechanism of action in which CecA binds to and covers the membrane surface, thereby causing a general destabilization and leakiness of the lipid bilayer membrane. The data are discussed in relation to a proposed mechanism of membrane lysis and bacterial killing via an ion channel activity of CecA.
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