Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide
dc.rights.license | open | en_US |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | JOBIN, Marie-Lise | |
dc.contributor.author | VAMPARYS, Lydie | |
dc.contributor.author | DENIAU, Romain | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | GRELARD, Axelle | |
hal.structure.identifier | Régulations Naturelles et Artificielles [ARNA] | |
dc.contributor.author | MACKERETH, Cameron D. | |
hal.structure.identifier | Laboratoire des biomolécules [LBM UMR 7203] | |
dc.contributor.author | FUCHS, Patrick F. J. | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | ALVES, Isabel | |
dc.date.accessioned | 2020-05-18T15:18:40Z | |
dc.date.available | 2020-05-18T15:18:40Z | |
dc.date.issued | 2019 | |
dc.identifier.issn | 1661-6596 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/7622 | |
dc.description.abstractEn | Cell-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.iso | EN | en_US |
dc.subject.en | cell-penetrating peptide | |
dc.subject.en | peptide–lipid interaction | |
dc.subject.en | lipid model systems | |
dc.subject.en | molecular dynamics | |
dc.subject.en | NMR | |
dc.subject.en | membrane biophysics | |
dc.title.en | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide | |
dc.title.alternative | itms | en_US |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.3390/ijms20184441 | |
dc.subject.hal | Chimie/Matériaux | en_US |
bordeaux.journal | International Journal of Molecular Sciences | en_US |
bordeaux.page | 21 p. | en_US |
bordeaux.volume | 20 | en_US |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | en_US |
bordeaux.issue | 18 | en_US |
bordeaux.institution | Bordeaux INP | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
hal.identifier | hal-03160308 | |
hal.version | 1 | |
hal.date.transferred | 2021-03-26T10:02:48Z | |
hal.export | true | |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=International%20Journal%20of%20Molecular%20Sciences&rft.date=2019&rft.volume=20&rft.issue=18&rft.spage=21%20p.&rft.epage=21%20p.&rft.eissn=1661-6596&rft.issn=1661-6596&rft.au=JOBIN,%20Marie-Lise&VAMPARYS,%20Lydie&DENIAU,%20Romain&GRELARD,%20Axelle&MACKERETH,%20Cameron%20D.&rft.genre=article |
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