Melittin modifies bending elasticity in an unexpected way
| Autor: | Philippe Méléard, Nina Barbier, Claire Gerbeaud, Tanja Pott |
|---|---|
| Přispěvatelé: | Institut des Sciences Chimiques de Rennes (ISCR), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Diacylglycerophosphatidylcholine
Lipid Bilayers Antimicrobial peptides Peptide Bending elasticity [CHIM.INOR]Chemical Sciences/Inorganic chemistry 010402 general chemistry Hemolysis 01 natural sciences Biochemistry Melittin Giant vesicles 03 medical and health sciences chemistry.chemical_compound Amphiphile Lipid bilayer Molecular Biology Unilamellar Liposomes 030304 developmental biology chemistry.chemical_classification 0303 health sciences Alamethicin Vesicle Organic Chemistry Magainin Cell Biology Melitten Elasticity Biomechanical Phenomena 0104 chemical sciences X-ray diffraction Lysis chemistry Phosphatidylcholines |
| Zdroj: | Chemistry and Physics of Lipids Chemistry and Physics of Lipids, Elsevier, 2015, 185, pp.99-108. ⟨10.1016/j.chemphyslip.2014.05.004⟩ Chemistry and Physics of Lipids, 2015, 185, pp.99-108. ⟨10.1016/j.chemphyslip.2014.05.004⟩ |
| ISSN: | 0009-3084 |
| Popis: | International audience; Understanding the molecular mechanism of the interaction of amphipathic and antimicrobial peptides with membranes is of fundamental interest, especially because of the potential of amphipathic peptides as therapeutics. The most studied amphipathic peptides in this context are certainly melittin, magainin and alamethicin, of which melittin is the only one to exhibit a powerful hemolytic and therefore toxic action. Herein we study the effect of the antimicrobial but hemolytic peptide melittin on the bending elasticity of giant unilamellar vesicles (GUVs). The results are compared to the effects of non-hemolytic amphipathic peptides such as alamethicin. We found that monomeric melittin acts very differently on the membrane mechanical properties. Strikingly, the difference is the most pronounced for low peptide concentrations, relevant for the hemolytic action. This gives some insight into the subtle nature of this peptide-membrane interaction. Furthermore, the results show that bending elasticity measurements might be a sensitive way to distinguish between lytic and non-lytic antimicrobial peptides. |
| Databáze: | OpenAIRE |
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