ArticleBiochimica et biophysica acta2009
Effects of arginine density on the membrane-bound structure of a cationic antimicrobial peptide from solid-state NMR.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria.International journal of molecular sciences · 2019Article
- Binding and Flip as Initial Steps for BP-100 Antimicrobial Actions.Scientific reports · 2019Article
- MASBiophysical journal · 2016Article
- Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c.Biophysical journal · 2015Article
- Modification of β-Defensin-2 by Dicarbonyls Methylglyoxal and Glyoxal Inhibits Antibacterial and Chemotactic Function In Vitro.PloS one · 2015Article
- Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs.Antibiotics (Basel, Switzerland) · 2014Article
- Mutations in BIN1 associated with centronuclear myopathy disrupt membrane remodeling by affecting protein density and oligomerization.PloS one · 2014Article
- Determining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Journal of biomolecular NMR · 2013Article
- Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine- and valine-rich β-hairpin-like antimicrobial peptides.Antimicrobial agents and chemotherapy · 2012Article
- Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Protein science : a publication of the Protein Society · 2011Article
- Article
- The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.Biochemistry · 2010Article
- Coupling between the voltage-sensing and phosphatase domains of Ci-VSP.The Journal of general physiology · 2009Article
- Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.Molecular bioSystems · 2009Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Solid-state NMR spectroscopy is used to determine the membrane-bound topological structure of a cationic beta-hairpin antimicrobial peptide in which the number of Arg residues has been halved. The parent peptide, PG-1, was previously found to form transmembrane beta-barrels in anionic membranes where the Arg residues complex with the lipid phosphate groups to cause toroidal pore defects in the membrane. In comparison, the charge-attenuated and less active mutant studied here forms beta-sheets that lie on the surface of the zwitterionic membrane and only partially insert into the anionic membrane. The mutant also exhibits much looser contact with the lipid headgroups. These results indicate that transmembrane insertion and tight Arg-phosphate association are two important elements for strong antimicrobial activities of this class of peptides. Comparison with other beta-hairpin antimicrobial peptides studied so far further suggests a relative potency scale for the various mechanisms of action for the beta-sheet family of antimicrobial peptides. The transmembrane insertion-toroidal pore mechanism is the most potent in disrupting the lipid bilayer, followed by the large-amplitude in-plane motional mechanism. The carpet model, where peptides aggregate on the membrane surface to cause lateral expansion and eventual micellization of the membrane, is a weaker mechanism of action.
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