ArticleThe journal of physical chemistry. B2007
Cation-pi interactions stabilize the structure of the antimicrobial peptide indolicidin near membranes: molecular dynamics simulations.
Article in The journal of physical chemistry. B, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 86 citations in OpenAlex.
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Article
- Nanosystems for delivery of indolicidin peptide.Frontiers in medical technology · 2026Review
- Binding of Antimicrobial Peptide Indolicidin to DMPC Bilayer Using Replica-Exchange Molecular Dynamics.Journal of chemical information and modeling · 2025Article
- Structure-based design of an antibacterial peptide from the Myotoxin II sequence, evaluating its effectiveness against Gram-negative bacteria and its safety.Scientific reports · 2025Article
- Augmentation of Antimicrobial Activity of Spiniferin by Introducing an Arginine Residue Toward Its Amino Terminus: A Possible Role of Cation-π Interaction.ACS bio & med chem Au · 2025Article
- Anti-Biofilm Effects of Rationally Designed Peptides against Planktonic Cells and Pre-Formed Biofilm ofAntibiotics (Basel, Switzerland) · 2023Article
- Atomic Force Microscopy to Characterize Antimicrobial Peptide-Induced Defects in Model Supported Lipid Bilayers.Microorganisms · 2021Article
- Conformational Characterization of the Co-Activator Binding Site Revealed the Mechanism to Achieve the Bioactive State of FXR.Frontiers in molecular biosciences · 2021Article
- Trp-Containing Antibacterial Peptides Impair Quorum Sensing and Biofilm Development in Multidrug-ResistantFrontiers in microbiology · 2021Article
- Are Antimicrobial Peptide Dendrimers an Escape from ESKAPE?Advances in wound care · 2020Article
- Development of potent CPP6-gemcitabine conjugates against human prostate cancer cell line (PC-3).RSC medicinal chemistry · 2020Article
- Synergistic Antibacterial Activity of Designed Trp-Containing Antibacterial Peptides in Combination With Antibiotics Against Multidrug-ResistantFrontiers in microbiology · 2019Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Tryptophan-Rich and Proline-Rich Antimicrobial Peptides.Molecules (Basel, Switzerland) · 2018Review
- Computational studies of peptide-induced membrane pore formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Synthesis and molecular docking studies of xanthone attached amino acids as potential antimicrobial and anti-inflammatory agents.MedChemComm · 2017Article
- Design and surface immobilization of short anti-biofilm peptides.Acta biomaterialia · 2017Article
- Archetypal tryptophan-rich antimicrobial peptides: properties and applications.World journal of microbiology & biotechnology · 2016Review
- Peptides and Peptidomimetics for Antimicrobial Drug Design.Pharmaceuticals (Basel, Switzerland) · 2015Review
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 1 institution in 1 country.
Funding
Abstract
We implemented molecular dynamics simulations of the 13-residue antimicrobial peptide indolicidin (ILPWKWPWWPWRR-NH2) in dodecylphosphocholine (DPC) and sodium dodecyl sulfate (SDS) micelles. In DPC, a persistent cation-pi interaction between TRP11 and ARG13 defined the structure of the peptide near the interface. A transient cation-pi interaction was also observed between TRP4 and the choline group on DPC lipids. We also implemented simulation of a mutant of indolicidin in the DPC micelle where TRP11 was replaced by ALA11. As a result of the mutation, the boat-shaped conformation is lost and the structure becomes significantly less defined. On the basis of this evidence, we argue that cation-pi interactions determine the experimentally measured, well-defined boat-shaped structure of indolicidin. In SDS, the lack of such interactions and the electrostatic binding of the terminal arginine residues to the sulfate groups leads to an extended peptide structure. To the best of our knowledge, this is the first time that a cation-pi interaction between peptide side chains has been shown to stabilize the structure of a small antimicrobial peptide. The simulations are in excellent agreement with available experimental measurements: the backbone of the peptide is more ordered in DPC than in SDS; the tryptophan side chains pack against the backbone in DPC and point away from the backbone in SDS; the rms fluctuation of the peptide backbone and peptide side chains is greater in SDS than in DPC; and the peptide backbone order parameters are higher in DPC than in SDS.
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.