ArticleBiophysical journal2012
Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- Binding and dimerization of PGLa peptides in anionic lipid bilayer studied by replica exchange molecular dynamics.Scientific reports · 2024Article
- Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential.Journal of chemical information and modeling · 2022Article
- Simulation Study of the Effect of Antimicrobial Peptide Associations on the Mechanism of Action with Bacterial and Eukaryotic Membranes.Membranes · 2022Article
- Mechanistic Understanding from Molecular Dynamics in Pharmaceutical Research 2: Lipid Membrane in Drug Design.Pharmaceuticals (Basel, Switzerland) · 2021Review
- pH-Dependent Conformations of an Antimicrobial Spider Venom Peptide, Cupiennin 1a, from Unbiased HREMD Simulations.ACS omega · 2021Article
- Article
- Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions.Biophysical journal · 2019Article
- Chirality-Dependent Adsorption between Amphipathic Peptide and POPC Membrane.International journal of molecular sciences · 2019Article
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.Biophysical journal · 2018Article
- Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Biomolecules · 2018Review
- Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2.Scientific reports · 2017Article
- Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.Biophysical journal · 2017Article
- Structural Behavior of the Peptaibol Harzianin HK VI in a DMPC Bilayer: Insights from MD Simulations.Biophysical journal · 2017Article
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 2016Article
- Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide.Nature communications · 2016Article
- Article
- Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes.European biophysics journal : EBJ · 2016Article
- Pore Structure and Synergy in Antimicrobial Peptides of the Magainin Family.PLoS computational biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane-active antimicrobial peptide PGLa from Xenopus laevis is known from solid-state (2)H-, (15)N-, and (19)F-NMR spectroscopy to occupy two distinct α-helical surface adsorbed states in membranes: a surface-bound S-state with a tilt angle of ~95° at low peptide/lipid molar ratio (P/L = 1:200), and an obliquely tilted T-state with a tilt angle of 127° at higher peptide concentration (P/L = 1:50). Using a rapid molecular-dynamics insertion protocol in combination with microsecond-scale simulation, we have characterized the structure of both states in detail. As expected, the amphiphilic peptide resides horizontally on the membrane surface in a monomeric form at a low P/L, whereas the T-state is seen in the simulations to be a symmetric antiparallel dimer, with close contacts between small glycine and alanine residues at the interface. The computed tilt angles and azimuthal rotations, as well as the quadrupolar splittings predicted from the simulations agree with the experimental NMR data. The simulations reveal many structural details previously inaccessible, such as the immersion depth of the peptide in the membrane and the packing of the dimerization interface. The study highlights the ability and limitations of current state-of-the-art multimicrosecond all-atom simulations of membrane-active peptides to complement experimental data from solid-state NMR.
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