ArticleBiophysical journal2000
Protein-induced membrane disorder: a molecular dynamics study of melittin in a dipalmitoylphosphatidylcholine bilayer.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 91 citations in OpenAlex.
- Structural Phenomena in a Vesicle Membrane Obtained through an Evolution Experiment: A Study Based on MD Simulations.Life (Basel, Switzerland) · 2023Article
- Mechanistic Landscape of Membrane-Permeabilizing Peptides.Chemical reviews · 2019Review
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
- Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.Biophysical journal · 2012Article
- Molecular dynamics simulation of Bombolitin II in the dipalmitoylphosphatidylcholine membrane bilayer.Biophysical journal · 2011Article
- Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Cellular and molecular life sciences : CMLS · 2011Review
- Protein folding in a reverse micelle environment: the role of confinement and dehydration.The Journal of chemical physics · 2011Article
- Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.Biophysical journal · 2010Article
- Computational modeling of poly(alkylthiophene) conductive polymer insertion into phospholipid bilayers.Langmuir : the ACS journal of surfaces and colloids · 2007Article
- Orientation and dynamics of melittin in membranes of varying composition utilizing NBD fluorescence.Biophysical journal · 2007Article
- Diffraction-based density restraints for membrane and membrane-peptide molecular dynamics simulations.Biophysical journal · 2006Article
- A molecular dynamics study of the bee venom melittin in aqueous solution, in methanol, and inserted in a phospholipid bilayer.European biophysics journal : EBJ · 2006Article
- Effect of hexafluoroisopropanol alcohol on the structure of melittin: a molecular dynamics simulation study.Protein science : a publication of the Protein Society · 2005Article
- Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein.Biophysical journal · 2005Article
- Molecular dynamics simulations of the lipid bilayer edge.Biophysical journal · 2004Article
- An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins.Biophysical journal · 2003Article
- Assessing the effects of time and spatial averaging in 15N chemical shift/15N-1H dipolar correlation solid state NMR experiments.Journal of biomolecular NMR · 2003Article
- Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular-dynamics simulations.The Biochemical journal · 2003Article
- Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A molecular dynamics simulation of melittin in a hydrated dipalmitoylphosphatidylcholine (DPPC) bilayer was performed. The 19, 000-atom system included a 72-DPPC phospholipid bilayer, a 26-amino acid peptide, and more than 3000 water molecules. The N-terminus of the peptide was protonated and embedded in the membrane in a transbilayer orientation perpendicular to the surface. The simulation results show that the peptide affects the lower (intracellular) layer of the bilayer more strongly than the upper (extracellular) layer. The simulation results can be interpreted as indicating an increased level of disorder and structural deformation for lower-layer phospholipids in the immediate vicinity of the peptide. This conclusion is supported by the calculated deuterium order parameters, the observed deformation at the intracellular interface, and an increase in fractional free volume. The upper layer was less affected by the embedded peptide, except for an acquired tilt relative to the bilayer normal. The effect of melittin on the surrounding membrane is localized to its immediate vicinity, and its asymmetry with respect to the two layers may result from the fact that it is not fully transmembranal. Melittin's hydrophilic C-terminus anchors it at the extracellular interface, leaving the N-terminus "loose" in the lower layer of the membrane. In general, the simulation supports a role for local deformation and water penetration in melittin-induced lysis. As for the peptide, like other membrane-embedded polypeptides, melittin adopts a significant 25 degree tilt relative to the membrane normal. This tilt is correlated with a comparable tilt of the lipids in the upper membrane layer. The peptide itself retains an overall helical structure throughout the simulation (with the exception of the three N-terminal residues), adopting a 30 degree intrahelical bend angle.
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