ArticleBiophysical journal2001
Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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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.
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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.
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Who cites it
57 citing papers in PubMed, 155 citations in OpenAlex.
- Antimicrobial peptides: An important link in the game theory between plants and pathogens.Journal of advanced research · 2026Review
- Antimicrobial Peptide Activity in Lipid Bilayers with Smooth-Type Lipopolysaccharides.Analytical chemistry · 2026Article
- Antimicrobial peptide resistance in Salmonella AMR: the role of surface binding and lipopolysaccharide remodelling: one health implications.World journal of microbiology & biotechnology · 2026Review
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- The Invertebrate-Derived Antimicrobial Peptide Cm-p5 Induces Cell Death and ROS Production in Melanoma Cells.Marine drugs · 2025Article
- Charge, Hydrophobicity, and Lipid Type Drive Antimicrobial Peptides' Unique Perturbation Ensembles.Biochemistry · 2025Article
- Dissecting Structural Requirements of Leucinostatin A Derivatives for Antiprotozoal Activity and Mammalian Toxicity.Journal of medicinal chemistry · 2025Article
- From oncolytic peptides to oncolytic polymers: A new paradigm for oncotherapy.Bioactive materials · 2024Review
- Mechanistic Insight into the Early Stages of Toroidal Pore Formation by the Antimicrobial Peptide Smp24.Pharmaceutics · 2023Article
- Liposome Deformation Induced by Membrane-Binding Peptides.Micromachines · 2023Article
- Peptaibols: Diversity, bioactivity, and biosynthesis.Engineering microbiology · 2022Review
- Antimicrobial Peptide Combination Can Hinder Resistance Evolution.Microbiology spectrum · 2022Article
- A mini-review: mechanism of antimicrobial action and application of surfactin.World journal of microbiology & biotechnology · 2022Review
- Mechanistic Evaluation of Antimicrobial Lipid Interactions with Tethered Lipid Bilayers by Electrochemical Impedance Spectroscopy.Sensors (Basel, Switzerland) · 2022Article
- Active SBiochimica et biophysica acta. Biomembranes · 2020Article
- 14-Helical β-Peptides Elicit Toxicity against C. albicans by Forming Pores in the Cell Membrane and Subsequently Disrupting Intracellular Organelles.Cell chemical biology · 2019Article
- The Use of Tethered Bilayer Lipid Membranes to Identify the Mechanisms of Antimicrobial Peptide Interactions with Lipid Bilayers.Antibiotics (Basel, Switzerland) · 2019Review
- Enhancing the signal strength of surface sensitive 2D IR spectroscopy.The Journal of chemical physics · 2019Article
- Therapeutic Potential of a Scorpion Venom-Derived Antimicrobial Peptide and Its Homologs Against Antibiotic-Resistant Gram-Positive Bacteria.Frontiers in microbiology · 2018Article
- What can machine learning do for antimicrobial peptides, and what can antimicrobial peptides do for machine learning?Interface focus · 2017Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The orientation and dynamics of an 18-residue antimicrobial peptide, ovispirin, has been investigated using solid-state NMR spectroscopy. Ovispirin is a cathelicidin-like model peptide (NH(2)-KNLRRIIRKIIHIIKKYG-COOH) with potent, broad-spectrum bactericidal activity. (15)N NMR spectra of oriented ovispirin reconstituted into synthetic phospholipids show that the helical peptide is predominantly oriented in the plane of the lipid bilayer, except for a small portion of the helix, possibly at the C-terminus, which deviates from the surface orientation. This suggests differential insertion of the peptide backbone into the lipid bilayer. (15)N spectra of both oriented and unoriented peptides show a reduced (15)N chemical shift anisotropy at room temperature compared with that of rigid proteins, indicating that the peptide undergoes uniaxial rotational diffusion around the bilayer normal with correlation times shorter than 10(-4) s. This motion is frozen below the gel-to-liquid crystalline transition temperature of the lipids. Ovispirin interacts strongly with the lipid bilayer, as manifested by the significantly reduced (2)H quadrupolar splittings of perdeuterated palmitoyloleoylphosphatidylcholine acyl chains upon peptide binding. Therefore, ovispirin is a curved helix residing in the membrane-water interface that executes rapid uniaxial rotation. These structural and dynamic features are important for understanding the antimicrobial function of this peptide.
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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.