JOBIN, Marie-Lise; VAMPARYS, Lydie; DENIAU, Romain; GRELARD, Axelle; MACKERETH, Cameron D.; FUCHS, Patrick F. J.; ALVES, Isabel

doi:10.3390/ijms20184441

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JOBIN, Marie-Lise

Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

VAMPARYS, Lydie

DENIAU, Romain

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International Journal of Molecular Sciences. 2019, vol. 20, n° 18, p. 21 p.

Résumé en anglais

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.< Réduire

Mots clés en anglais

cell-penetrating peptide

peptide–lipid interaction

lipid model systems

molecular dynamics

NMR

membrane biophysics

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

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