gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

Giovanni Smaldone,1,2 Annarita Falanga,3 Domenica Capasso,4 Daniela Guarnieri,5,6 Stefania Correale,1,7 Massimiliano Galdiero,8 Paolo A Netti,4 Massimo Zollo,9 Stefania Galdiero,1,2 Sonia Di Gaetano,1 Emilia Pedone1 1Institute of Biostructures and Bioimaging, National Research Council, Naples, Italy...

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Autores principales:	Smaldone G, Falanga A, Capasso D, Guarnieri D, Correale S, Galdiero M, Netti PA, Zollo M, Galdiero S, Di Gaetano S, Pedone E
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2013
Materias:	Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/7bf3cc1d0cbb49e7b24f55af461371e2
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spelling	oai:doaj.org-article:7bf3cc1d0cbb49e7b24f55af461371e22021-12-02T00:43:06ZgH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins1176-91141178-2013https://doaj.org/article/7bf3cc1d0cbb49e7b24f55af461371e22013-07-01T00:00:00Zhttp://www.dovepress.com/gh625-is-a-viral-derived-peptide-for-effective-delivery-of-intrinsical-a13738https://doaj.org/toc/1176-9114https://doaj.org/toc/1178-2013Giovanni Smaldone,1,2 Annarita Falanga,3 Domenica Capasso,4 Daniela Guarnieri,5,6 Stefania Correale,1,7 Massimiliano Galdiero,8 Paolo A Netti,4 Massimo Zollo,9 Stefania Galdiero,1,2 Sonia Di Gaetano,1 Emilia Pedone1 1Institute of Biostructures and Bioimaging, National Research Council, Naples, Italy; 2Department of Pharmacy and Interuniversity Research Center on Bioactive Peptides, Federico II University of Naples, Naples, Italy; 3Molecular Diagnostics and Pharmaceuticals Scarl, Naples, Italy; 4Special Center for Biotechnology, Federico II University of Naples, Naples, Italy; 5Center for Advanced Biomaterials for Health Care, Interdisciplinary Research Centre on Biomaterials, Italian Institute of Technology, Naples, Italy; 6Interdisciplinary Research Centre on Biomaterials, Federico II University of Naples, Naples, Italy; 7Kedrion S.p.A, Sant'antimo, Naples, Italy; 8Department of Experimental Medicine, Federico II University of Naples, Naples, Italy; 9CEINGE – Advanced Biotechnology Scarl, Naples, Italy Abstract: A genetically modified recombinant gH625-c-prune was prepared through conjugation of c-prune with gH625, a peptide encompassing 625–644 residues of the glycoprotein H of herpes simplex virus 1, which has been proved to possess the ability to carry cargo molecules across cell membranes. C-prune is the C-terminal domain of h-prune, overexpressed in breast, colorectal, and gastric cancers, interacting with multiple partners, and representing an ideal target for inhibition of cancer development. Its C-terminal domain results in an intrinsically disordered domain (IDD), and the peculiar properties of gH625 render it an optimal candidate to act as a carrier for this net negatively charged molecule by comparison with the positively charged TAT. A characterization of the recombinant gH625-c-prune fusion protein was conducted by biochemical, cellular biology and confocal microscopy means in comparison with TAT-c-prune. The results showed that the gH625-c-prune exhibited the ability to cross biomembranes, opening a new scenario on the use of gH625 as a novel multifunctional carrier. Keywords: delivery, IDPSmaldone GFalanga ACapasso DGuarnieri DCorreale SGaldiero MNetti PAZollo MGaldiero SDi Gaetano SPedone EDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2013, Iss default, Pp 2555-2565 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine (General) R5-920
spellingShingle	Medicine (General) R5-920 Smaldone G Falanga A Capasso D Guarnieri D Correale S Galdiero M Netti PA Zollo M Galdiero S Di Gaetano S Pedone E gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
description	Giovanni Smaldone,1,2 Annarita Falanga,3 Domenica Capasso,4 Daniela Guarnieri,5,6 Stefania Correale,1,7 Massimiliano Galdiero,8 Paolo A Netti,4 Massimo Zollo,9 Stefania Galdiero,1,2 Sonia Di Gaetano,1 Emilia Pedone1 1Institute of Biostructures and Bioimaging, National Research Council, Naples, Italy; 2Department of Pharmacy and Interuniversity Research Center on Bioactive Peptides, Federico II University of Naples, Naples, Italy; 3Molecular Diagnostics and Pharmaceuticals Scarl, Naples, Italy; 4Special Center for Biotechnology, Federico II University of Naples, Naples, Italy; 5Center for Advanced Biomaterials for Health Care, Interdisciplinary Research Centre on Biomaterials, Italian Institute of Technology, Naples, Italy; 6Interdisciplinary Research Centre on Biomaterials, Federico II University of Naples, Naples, Italy; 7Kedrion S.p.A, Sant'antimo, Naples, Italy; 8Department of Experimental Medicine, Federico II University of Naples, Naples, Italy; 9CEINGE – Advanced Biotechnology Scarl, Naples, Italy Abstract: A genetically modified recombinant gH625-c-prune was prepared through conjugation of c-prune with gH625, a peptide encompassing 625–644 residues of the glycoprotein H of herpes simplex virus 1, which has been proved to possess the ability to carry cargo molecules across cell membranes. C-prune is the C-terminal domain of h-prune, overexpressed in breast, colorectal, and gastric cancers, interacting with multiple partners, and representing an ideal target for inhibition of cancer development. Its C-terminal domain results in an intrinsically disordered domain (IDD), and the peculiar properties of gH625 render it an optimal candidate to act as a carrier for this net negatively charged molecule by comparison with the positively charged TAT. A characterization of the recombinant gH625-c-prune fusion protein was conducted by biochemical, cellular biology and confocal microscopy means in comparison with TAT-c-prune. The results showed that the gH625-c-prune exhibited the ability to cross biomembranes, opening a new scenario on the use of gH625 as a novel multifunctional carrier. Keywords: delivery, IDP
format	article
author	Smaldone G Falanga A Capasso D Guarnieri D Correale S Galdiero M Netti PA Zollo M Galdiero S Di Gaetano S Pedone E
author_facet	Smaldone G Falanga A Capasso D Guarnieri D Correale S Galdiero M Netti PA Zollo M Galdiero S Di Gaetano S Pedone E
author_sort	Smaldone G
title	gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
title_short	gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
title_full	gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
title_fullStr	gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
title_full_unstemmed	gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
title_sort	gh625 is a viral derived peptide for effective delivery of intrinsically disordered proteins
publisher	Dove Medical Press
publishDate	2013
url	https://doaj.org/article/7bf3cc1d0cbb49e7b24f55af461371e2
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gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

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