dorsal/arxiv
View SchemaDefect formation of lytic peptides in lipid membranes and their influence on the thermodynamic properties of the pore environment
| Authors | Vitaliy Oliynyk, Udo Kaatze, Thomas Heimburg |
|---|---|
| Categories | |
| ArXiv ID | physics/0609054 |
| URL | https://arxiv.org/abs/physics/0609054 |
| DOI | 10.1016/j.bbamem.2006.10.007 |
| Journal | Biochim. Biophys. Acta 1768 (2007) 236-245 |
Abstract
We present an experimental study of the pore formation processes of small amphipathic peptides in model phosphocholine lipid membranes. We used atomic force microscopy to characterize the spatial organization and structure of alamethicin- and melittin- induced defects in lipid bilayer membranes and the influence of the peptide on local membrane properties. Alamethicin induced holes in gel DPPC membranes were directly visualized at different peptide concentrations. We found that the thermodynamic state of lipids in gel membranes can be influenced by the presence of alamethicin such that nanoscopic domains of fluid lipids form close to the peptide pores, and that the elastic constants of the membrane are altered in their vicinity. Melittin-induced holes were visualized in DPPC and DLPC membranes at room temperature in order to study the influence of the membrane state on the peptide induced hole formation. Also differential scanning calorimetry was used to investigate the effect of alamethicin on the lipid membrane phase behavior.
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"abstract": "We present an experimental study of the pore formation processes of small\namphipathic peptides in model phosphocholine lipid membranes. We used atomic\nforce microscopy to characterize the spatial organization and structure of\nalamethicin- and melittin- induced defects in lipid bilayer membranes and the\ninfluence of the peptide on local membrane properties. Alamethicin induced\nholes in gel DPPC membranes were directly visualized at different peptide\nconcentrations. We found that the thermodynamic state of lipids in gel\nmembranes can be influenced by the presence of alamethicin such that nanoscopic\ndomains of fluid lipids form close to the peptide pores, and that the elastic\nconstants of the membrane are altered in their vicinity. Melittin-induced holes\nwere visualized in DPPC and DLPC membranes at room temperature in order to\nstudy the influence of the membrane state on the peptide induced hole\nformation. Also differential scanning calorimetry was used to investigate the\neffect of alamethicin on the lipid membrane phase behavior.",
"arxiv_id": "physics/0609054",
"authors": [
"Vitaliy Oliynyk",
"Udo Kaatze",
"Thomas Heimburg"
],
"categories": [
"physics.bio-ph"
],
"doi": "10.1016/j.bbamem.2006.10.007",
"journal_ref": "Biochim. Biophys. Acta 1768 (2007) 236-245",
"title": "Defect formation of lytic peptides in lipid membranes and their influence on the thermodynamic properties of the pore environment",
"url": "https://arxiv.org/abs/physics/0609054"
},
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