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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6769507/ https://www.ncbi.nlm.nih.gov/pubmed/31505894 http://dx.doi.org/10.3390/ijms20184441 |
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author | Jobin, Marie-Lise Vamparys, Lydie Deniau, Romain Grélard, Axelle Mackereth, Cameron D. Fuchs, Patrick F.J. Alves, Isabel D. |
author_facet | Jobin, Marie-Lise Vamparys, Lydie Deniau, Romain Grélard, Axelle Mackereth, Cameron D. Fuchs, Patrick F.J. Alves, Isabel D. |
author_sort | Jobin, Marie-Lise |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6769507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-67695072019-10-30 Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide Jobin, Marie-Lise Vamparys, Lydie Deniau, Romain Grélard, Axelle Mackereth, Cameron D. Fuchs, Patrick F.J. Alves, Isabel D. Int J Mol Sci Article 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. MDPI 2019-09-09 /pmc/articles/PMC6769507/ /pubmed/31505894 http://dx.doi.org/10.3390/ijms20184441 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Jobin, Marie-Lise Vamparys, Lydie Deniau, Romain Grélard, Axelle Mackereth, Cameron D. Fuchs, Patrick F.J. Alves, Isabel D. Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title_full | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title_fullStr | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title_full_unstemmed | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title_short | Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide |
title_sort | biophysical insight on the membrane insertion of an arginine-rich cell-penetrating peptide |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6769507/ https://www.ncbi.nlm.nih.gov/pubmed/31505894 http://dx.doi.org/10.3390/ijms20184441 |
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