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Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide

dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorJOBIN, Marie-Lise
dc.contributor.authorVAMPARYS, Lydie
dc.contributor.authorDENIAU, Romain
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGRELARD, Axelle
hal.structure.identifierRégulations Naturelles et Artificielles [ARNA]
dc.contributor.authorMACKERETH, Cameron D.
hal.structure.identifierLaboratoire des biomolécules [LBM UMR 7203]
dc.contributor.authorFUCHS, Patrick F. J.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorALVES, Isabel
dc.date.accessioned2020-05-18T15:18:40Z
dc.date.available2020-05-18T15:18:40Z
dc.date.issued2019
dc.identifier.issn1661-6596en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7622
dc.description.abstractEnCell-penetrating peptides (CPPs) are short peptides that can translocate and transport cargoes into the intracellular milieu by crossing biological membranes. The mode of interaction and internalization of cell-penetrating peptides has long been controversial. While their interaction with anionic membranes is quite well understood, the insertion and behavior of CPPs in zwitterionic membranes, a major lipid component of eukaryotic cell membranes, is poorly studied. Herein, we investigated the membrane insertion of RW16 into zwitterionic membranes, a versatile CPP that also presents antibacterial and antitumor activities. Using complementary approaches, including NMR spectroscopy, fluorescence spectroscopy, circular dichroism, and molecular dynamic simulations, we determined the high-resolution structure of RW16 and measured its membrane insertion and orientation properties into zwitterionic membranes. Altogether, these results contribute to explaining the versatile properties of this peptide toward zwitterionic lipids.
dc.language.isoENen_US
dc.subject.encell-penetrating peptide
dc.subject.enpeptide–lipid interaction
dc.subject.enlipid model systems
dc.subject.enmolecular dynamics
dc.subject.enNMR
dc.subject.enmembrane biophysics
dc.title.enBiophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide
dc.title.alternativeitmsen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/ijms20184441
dc.subject.halChimie/Matériauxen_US
bordeaux.journalInternational Journal of Molecular Sciencesen_US
bordeaux.page21 p.en_US
bordeaux.volume20en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue18en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03160308
hal.version1
hal.date.transferred2021-03-26T10:02:48Z
hal.exporttrue
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