| Autor: |
Jobin ML; Institute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France. marie-lise.jobin@u-bordeaux.fr.; Present address: Interdisciplinary Institute for Neuroscience (IINS), CNRS UMR5297, University of Bordeaux, 33000 Bordeaux, France. marie-lise.jobin@u-bordeaux.fr., Vamparys L; University of Paris, Institut Jacques Monod, CNRS, 75013 Paris, France., Deniau R; University of Paris, Institut Jacques Monod, CNRS, 75013 Paris, France., Grélard A; Institute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France., Mackereth CD; INSERM U1212, CNRS UMR5320, ARNA Laboratory, University of Bordeaux, IECB, 2 rue Robert Escarpit, 33600 Pessac, France., Fuchs PFJ; Sorbonne University, École normale supérieure, PSL University, CNRS, Laboratoire des biomolécules (LBM), 75005 Paris, France.; University of Paris, UFR Sciences du Vivant, 75013 Paris, France., Alves ID; Institute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), CNRS UMR5248, University of Bordeaux, Bordeaux INP, allée Geoffroy St-Hilaire, 33600 Pessac, France. i.alves@cbmn.u-bordeaux.fr. |
| Abstrakt: |
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. |
