ArticleBiophysical journal2007
Antimicrobial peptide-lipid binding interactions and binding selectivity.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 82 citations in OpenAlex.
- Noncanonical bactericidal activity of teleost type I interferon is conferred by a membrane-targeting C-terminal peptide.PLoS pathogens · 2026Article
- Identification and Characterization of an In Silico Designed Membrane-Active Peptide with Antiviral Properties.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Melittin-Induced Structural Transformations in DMPG and DMPS Lipid Membranes: A Langmuir Monolayer and AFM Study.Molecules (Basel, Switzerland) · 2024Article
- Marine Invertebrate Antimicrobial Peptides and Their Potential as Novel Peptide Antibiotics.Marine drugs · 2023Review
- Polymyxins induce lipid scrambling and disrupt the homeostasis of Gram-negative bacteria membrane.Biophysical journal · 2022Article
- Article
- Antimicrobial Peptides as Probes in Biosensors Detecting Whole Bacteria: A Review.Molecules (Basel, Switzerland) · 2020Review
- Trematocine, a Novel Antimicrobial Peptide from the Antarctic FishAntibiotics (Basel, Switzerland) · 2020Article
- High-throughput photoelectrochemical determination of E. coli O157:H7 by modulation of the anodic photoelectrochemistry of CdS quantum dots via reversible deposition of MnOMikrochimica acta · 2019Article
- Influence of Acyl Chain Saturation on the Membrane-Binding Activity of a Short Antimicrobial Peptide.ACS omega · 2017Article
- Potent in vitro and in vivo antifungal activity of a small molecule host defense peptide mimic through a membrane-active mechanism.Scientific reports · 2017Article
- Interaction of the antimicrobial peptide polymyxin B1 with both membranes of E. coli: a molecular dynamics study.PLoS computational biology · 2015Article
- Energetic view on membrane pore formation.Biophysical journal · 2014Article
- Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae.International journal of medicinal chemistry · 2014Article
- Common mechanism unites membrane poration by amyloid and antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Low resolution structure and dynamics of a colicin-receptor complex determined by neutron scattering.The Journal of biological chemistry · 2012Article
- Electrical detection of pathogenic bacteria via immobilized antimicrobial peptides.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Exploring the membrane mechanism of the bioactive peptaibol ampullosporin a using lipid monolayers and supported biomimetic membranes.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2010Article
- Interfacial assembly of proteins and peptides: recent examples studied by neutron reflection.Journal of the Royal Society, Interface · 2009Review
- Molecular interactions between magainin 2 and model membranes in situ.The journal of physical chemistry. B · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Surface pressure measurements, external reflection-Fourier transform infrared spectroscopy, and neutron reflectivity have been used to investigate the lipid-binding behavior of three antimicrobial peptides: melittin, magainin II, and cecropin P1. As expected, all three cationic peptides were shown to interact more strongly with the anionic lipid, 1,2 dihexadecanoyl-sn-glycerol-3-(phosphor-rac-(1-glycerol)) (DPPG), compared to the zwitterionic lipid, 1,2 dihexadecanoyl-sn-glycerol-3-phosphocholine (DPPC). All three peptides have been shown to penetrate DPPC lipid layers by surface pressure, and this was confirmed for the melittin-DPPC interaction by neutron reflectivity measurements. Adsorption of peptide was, however, minimal, with a maximum of 0.4 mg m(-2) seen for melittin adsorption compared to 2.1 mg m(-2) for adsorption to DPPG (from 0.7 microM solution). The mode of binding to DPPG was shown to depend on the distribution of basic residues within the peptide alpha-helix, although in all cases adsorption below the lipid layer was shown to dominate over insertion within the layer. Melittin adsorption to DPPG altered the lipid layer structure observed through changes in the external reflection-Fourier transform infrared lipid spectra and neutron reflectivity. This lipid disruption was not observed for magainin or cecropin. In addition, melittin binding to both lipids was shown to be 50% greater than for either magainin or cecropin. Adsorption to the bare air-water interface was also investigated and surface activity followed the trend melittin>magainin>cecropin. External reflection-Fourier transform infrared amide spectra revealed that melittin adopted a helical structure only in the presence of lipid, whereas magainin and cecropin adopted helical structure also at an air-water interface. This behavior has been related to the different charge distributions on the peptide amino acid sequences.
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