Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625

gH625 constitutes a promising delivery vehicle for the transport of therapeutic biomacromolecules across membrane barriers. We report an application of multivalency to create a complex nanosystem for delivery and to elucidate the mechanism of peptide-lipid bilayer interactions. Multivalency may offe...

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Autores principales: Falanga, Annarita, Valiante, Salvatore, Galdiero, Emilia, Franci, Gianluigi, Scudiero, Olga, Morelli, Giancarlo, Galdiero, Stefania
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5572722/
https://www.ncbi.nlm.nih.gov/pubmed/28842580
http://dx.doi.org/10.1038/s41598-017-09001-x
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author Falanga, Annarita
Valiante, Salvatore
Galdiero, Emilia
Franci, Gianluigi
Scudiero, Olga
Morelli, Giancarlo
Galdiero, Stefania
author_facet Falanga, Annarita
Valiante, Salvatore
Galdiero, Emilia
Franci, Gianluigi
Scudiero, Olga
Morelli, Giancarlo
Galdiero, Stefania
author_sort Falanga, Annarita
collection PubMed
description gH625 constitutes a promising delivery vehicle for the transport of therapeutic biomacromolecules across membrane barriers. We report an application of multivalency to create a complex nanosystem for delivery and to elucidate the mechanism of peptide-lipid bilayer interactions. Multivalency may offer a route to enhance gH625 cellular uptake as demonstrated by results obtained on dimers of gH625 by fluorescence spectroscopy, circular dichroism, and surface plasmon resonance. Moreover, using both phase contrast and light sheet fluorescence microscopy we were able to characterize and visualize for the first time the fusion of giant unilamellar vesicles caused by a membranotropic peptide.
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spelling pubmed-55727222017-09-01 Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625 Falanga, Annarita Valiante, Salvatore Galdiero, Emilia Franci, Gianluigi Scudiero, Olga Morelli, Giancarlo Galdiero, Stefania Sci Rep Article gH625 constitutes a promising delivery vehicle for the transport of therapeutic biomacromolecules across membrane barriers. We report an application of multivalency to create a complex nanosystem for delivery and to elucidate the mechanism of peptide-lipid bilayer interactions. Multivalency may offer a route to enhance gH625 cellular uptake as demonstrated by results obtained on dimers of gH625 by fluorescence spectroscopy, circular dichroism, and surface plasmon resonance. Moreover, using both phase contrast and light sheet fluorescence microscopy we were able to characterize and visualize for the first time the fusion of giant unilamellar vesicles caused by a membranotropic peptide. Nature Publishing Group UK 2017-08-25 /pmc/articles/PMC5572722/ /pubmed/28842580 http://dx.doi.org/10.1038/s41598-017-09001-x Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Falanga, Annarita
Valiante, Salvatore
Galdiero, Emilia
Franci, Gianluigi
Scudiero, Olga
Morelli, Giancarlo
Galdiero, Stefania
Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title_full Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title_fullStr Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title_full_unstemmed Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title_short Dimerization in tailoring uptake efficacy of the HSV-1 derived membranotropic peptide gH625
title_sort dimerization in tailoring uptake efficacy of the hsv-1 derived membranotropic peptide gh625
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5572722/
https://www.ncbi.nlm.nih.gov/pubmed/28842580
http://dx.doi.org/10.1038/s41598-017-09001-x
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