Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Antimicrobial peptide-lipid binding interactions and binding selectivity.

Mitaben D Lad1, Fabrice Birembaut, Luke A Clifton

  • 1School of Chemistry, Food Biosciences and Pharmacy, University of Reading, Whiteknights, Reading RG6 6AD, United Kingdom.

Biophysical Journal
|February 28, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Complex Structural Examination of Protein-Lipid Interactions with Neutron Scattering Techniques.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Twin-compartment solid-liquid cells for neutron reflectometry.

Journal of applied crystallography·2026
Same author

Avoiding Mitochondrial Apoptosis by the Bcl-2-Driven Bax Oligomerization on Membrane Surfaces.

ACS chemical biology·2026
Same author

Selective Serine Substitutions of Antimicrobial Peptides Reveal Different Mechanistic Actions Toward Gram-Negative Bacteria.

ACS applied materials & interfaces·2026
Same author

Lipo-oligo/polysaccharide biorecognition at the nano-bio interface: insights into LA27 aptamer binding to biomimetic bacterial membranes.

Journal of colloid and interface science·2025
Same author

Assessing the Mechanism of Action of Synthetic Nanoengineered Antimicrobial Polymers against the Bacterial Membrane of <i>Pseudomonas aeruginosa</i>.

Biomacromolecules·2025
Same journal

Tau protein differentially affects Piezo1 and Kir2.1 channels in brain capillary endothelial cells.

Biophysical journal·2026
Same journal

Emergent Intercellular Junction Stability during Cyclic Tissue Loading.

Biophysical journal·2026
Same journal

Enhanced-Sampling Simulations Reveal Distinct Intermediates in SARS-CoV-2 FSE Pseudoknot Interconversion.

Biophysical journal·2026
Same journal

Structure-based simulations of the full Flock House virus capsid reveal pathways and energetics of an infection-critical peptide externalization event.

Biophysical journal·2026
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
See all related articles

Antimicrobial peptides like melittin bind strongly to anionic lipids (DPPG) and disrupt their structure, while interactions with zwitterionic lipids (DPPC) are weaker. Melittin shows greater binding and surface activity than magainin II or cecropin P1.

Area of Science:

  • Biophysics
  • Biochemistry
  • Materials Science

Background:

  • Antimicrobial peptides (AMPs) are crucial for innate immunity.
  • Understanding AMP-lipid interactions is key to developing new therapeutics.
  • Lipid composition significantly influences AMP binding and activity.

Purpose of the Study:

  • To investigate the lipid-binding behavior of three AMPs: melittin, magainin II, and cecropin P1.
  • To compare their interactions with anionic (DPPG) and zwitterionic (DPPC) lipid layers.
  • To elucidate the structural changes induced by AMPs in lipid bilayers.

Main Methods:

  • Surface pressure measurements
  • External reflection-Fourier transform infrared spectroscopy (ER-FTIR)
  • Neutron reflectivity

Related Experiment Videos

Main Results:

  • All three cationic AMPs bound more strongly to anionic DPPG than zwitterionic DPPC.
  • Melittin significantly disrupted the DPPG lipid layer structure, unlike magainin II and cecropin P1.
  • Melittin exhibited greater binding affinity and surface activity compared to magainin II and cecropin P1.
  • Melittin adopted helical structure upon lipid interaction, while magainin II and cecropin P1 formed helices at the air-water interface.

Conclusions:

  • AMP binding and lipid disruption depend on lipid charge and peptide structure.
  • Melittin's unique interaction with anionic lipids suggests specific mechanisms of membrane disruption.
  • Differences in charge distribution influence AMP secondary structure formation and membrane activity.