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

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 me...

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Bibliographic Details
Published in:	International journal of molecular sciences Vol. 20; no. 18; p. 4441
Main Authors:	Jobin, Marie-Lise, Vamparys, Lydie, Deniau, Romain, Grélard, Axelle, Mackereth, Cameron D, Fuchs, Patrick F J, Alves, Isabel D
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 09-09-2019 MDPI
Subjects:	Arginine Arginine - chemistry Biochemistry, Molecular Biology Biological activity Biophysics Cell Membrane - chemistry Cell membranes cell-penetrating peptide Cell-Penetrating Peptides - chemistry Chemical Sciences Circular Dichroism Computer simulation Cytotoxicity Glycosaminoglycans Life Sciences lipid model systems Lipids Material chemistry membrane biophysics Membranes Micelles Molecular dynamics Molecular Dynamics Simulation Molecular structure NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Peptides peptide–lipid interaction Protein Structure, Secondary Spectroscopy Spectrum analysis NMR membrane biophysics lipid model systems molecular dynamics cell-penetrating peptide peptide–lipid interaction peptide-lipid interaction
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Interdisciplinary Institute for Neuroscience (IINS), CNRS UMR5297, University of Bordeaux, 33000 Bordeaux, France.
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms20184441