ArticleThe Biochemical journal2003
Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular-dynamics simulations.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed.
- Improving the antimicrobial activity of RP9 peptide through theoretical and experimental investigation.Biochemistry and biophysics reports · 2025Article
- Effect of monovalent salt concentration and peptide secondary structure in peptide-micelle binding.RSC advances · 2021Article
- Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activity.Scientific reports · 2020Article
- Article
- Correlated protein conformational states and membrane dynamics during attack by pore-forming toxins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Peptides and Peptidomimetics for Antimicrobial Drug Design.Pharmaceuticals (Basel, Switzerland) · 2015Review
- Interaction of the antimicrobial peptide polymyxin B1 with both membranes of E. coli: a molecular dynamics study.PLoS computational biology · 2015Article
- Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Journal of chemical theory and computation · 2013Article
- Comparative molecular dynamics simulations of the antimicrobial peptide CM15 in model lipid bilayers.Biochimica et biophysica acta · 2012Article
- Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.The journal of physical chemistry. B · 2011Article
- Electrostatics of deformable lipid membranes.Biophysical journal · 2010Article
- Determining the orientation of protegrin-1 in DLPC bilayers using an implicit solvent-membrane model.PloS one · 2009Article
- Pore formation induced by an antimicrobial peptide: electrostatic effects.Biophysical journal · 2008Article
- Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data.BMC biochemistry · 2007Article
- Molecular dynamics simulations of a stretch-activated channel inhibitor GsMTx4 with lipid membranes: two binding modes and effects of lipid structure.Biophysical journal · 2007Article
- Free energy profile of H-ras membrane anchor upon membrane insertion.Angewandte Chemie (International ed. in English) · 2007Article
- Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.Biophysical journal · 2006Article
- Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions.Biochimica et biophysica acta · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular-dynamics simulations covering 30 ns of both a natural and a synthetic antimicrobial peptide in the presence of a zwitterionic lipid bilayer were performed. In both simulations, copies of the peptides were placed in an alpha-helical conformation on either side of the bilayer about 10 A (1 A=0.1 nm) from the interface, with either the hydrophobic or the positively charged face of the helix directed toward the bilayer surface. The degree of peptide-lipid interaction was dependent on the starting configuration: surface binding and subsequent penetration of the bilayer was observed for the hydrophobically oriented peptides, while the charge-oriented peptides demonstrated at most partial surface binding. Aromatic residues near the N-termini of the peptides appear to play an important role in driving peptide-lipid interactions. A correlation between the extent of peptide-lipid interactions and helical stability was observed in the simulations. Insertion of the peptides into the bilayer caused a dramatic increase in the lateral area per lipid and decrease in the bilayer thickness, resulting in substantial disordering of the lipid chains. Results from the simulations are consistent with early stages of proposed mechanisms for the lytic activity of antimicrobial peptides. In addition to these 'free' simulations, 25 ns simulations were carried out with the peptides constrained at three different distances relative to the bilayer interface. The constraint forces are in agreement with the extent of peptide-bilayer insertion observed in the free simulations.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.