ArticleBiophysical journal2000
Atomic detail peptide-membrane interactions: molecular dynamics simulation of gramicidin S in a DMPC 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 13 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
13 citing papers in PubMed, 36 citations in OpenAlex.
- Rigidity vs Activity: Design of Gramicidin S Analogs against Multidrug-Resistant Bacteria Based on Molecular Engineering.Journal of medicinal chemistry · 2025Article
- An Electrospray Ionization Mass Spectrometry Study on the "In Vacuo" Hetero-Oligomers Formed by the Antimicrobial Peptides, Surfactin and Gramicidin S.Journal of the American Society for Mass Spectrometry · 2017Article
- Fermentation and Cost-Effective 13C/15N Labeling of the Nonribosomal Peptide Gramicidin S for Nuclear Magnetic Resonance Structure Analysis.Applied and environmental microbiology · 2015Article
- The high resolution structure of tyrocidine A reveals an amphipathic dimer.Biochimica et biophysica acta · 2014Article
- The molecular basis of ceramide-1-phosphate recognition by C2 domains.Journal of lipid research · 2013Article
- The molecular basis for antimicrobial activity of pore-forming cyclic peptides.Biophysical journal · 2011Article
- Therapeutic index of gramicidin S is strongly modulated by D-phenylalanine analogues at the beta-turn.Journal of medicinal chemistry · 2009Article
- Interaction of gramicidin S and its aromatic amino-acid analog with phospholipid membranes.Biophysical journal · 2008Article
- Differential roles of phosphatidylserine, PtdIns(4,5)P2, and PtdIns(3,4,5)P3 in plasma membrane targeting of C2 domains. Molecular dynamics simulation, membrane binding, and cell translocation studies of the PKCalpha C2 domain.The Journal of biological chemistry · 2008Article
- Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.Materials science & engineering. R, Reports : a review journal · 2007Article
- Atomically detailed folding simulation of the B domain of staphylococcal protein A from random structures.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Investigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations.Biophysical journal · 2003Article
- Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR.Journal of biomolecular NMR · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular dynamics simulations have been performed of the sequence-symmetric cyclic decapeptide antibiotic gramicidin S (GS), in interaction with a hydrated dimyristoylphosphatidylcholine (DMPC) bilayer, and the results compared with a "control" simulation of the system in the absence of GS. Following experimental evidence, the GS was initially set in a single antiparallel beta-sheet conformation with two Type II' beta-turns in an amphiphilic interaction with the membrane. This conformation and position remained in the 6.5 ns simulation. Main-chain dihedrals are on average approximately 26 degrees from those determined by NMR experiment on GS in dimethylsulfoxide (DMSO) solution. Sequence-symmetric main-chain and side-chain dihedral angle pairs converge to within approximately 5 degrees and approximately 10 degrees, respectively. The area per lipid, lipid tail order parameters, and quadrupole spin-lattice relaxation times of the control simulation are mostly in good agreement with corresponding experiments. The GS has little effect on the membrane dipole potential or water permeability. However, it is found to have a disordering effect (in agreement with experiment) and a fluidifying effect on lipids directly interacting with it, and an ordering effect on those not directly interacting.
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.