Dendrimers functionalized with membrane-interacting peptides for viral inhibition

Rossella Tarallo,1 Tom P Carberry,2 Annarita Falanga,1 Mariateresa Vitiello,3 Stefania Galdiero,1 Massimiliano Galdiero,3 Marcus Weck21Dipartimento di Farmacia, Università di Napoli "Federico II," and DFM Scarl, Napoli, Italia; 2Molecular Design Institute and...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Tarallo R, Carberry TP, Falanga A, Vitiello M, Galdiero S, Galdiero M, Weck M
Formato: article
Lenguaje:EN
Publicado: Dove Medical Press 2013
Materias:
Acceso en línea:https://doaj.org/article/56a726a661784ecf8b04be883ec88c0a
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:56a726a661784ecf8b04be883ec88c0a
record_format dspace
spelling oai:doaj.org-article:56a726a661784ecf8b04be883ec88c0a2021-12-02T03:11:38ZDendrimers functionalized with membrane-interacting peptides for viral inhibition1176-91141178-2013https://doaj.org/article/56a726a661784ecf8b04be883ec88c0a2013-02-01T00:00:00Zhttp://www.dovepress.com/dendrimers-functionalized-with-membrane-interacting-peptides-for-viral-a12134https://doaj.org/toc/1176-9114https://doaj.org/toc/1178-2013Rossella Tarallo,1 Tom P Carberry,2 Annarita Falanga,1 Mariateresa Vitiello,3 Stefania Galdiero,1 Massimiliano Galdiero,3 Marcus Weck21Dipartimento di Farmacia, Università di Napoli "Federico II," and DFM Scarl, Napoli, Italia; 2Molecular Design Institute and Department of Chemistry, New York University, New York, NY, USA; 3Dipartimento di Medicina Sperimentale, Seconda Università degli Studi di Napoli, Napoli, ItaliaAbstract: This contribution reports the synthesis of a poly(amide)-based dendrimer functionalized at the termini with a membrane-interacting peptide derived from the herpes simplex virus (HSV) type 1 glycoprotein H, namely gH625-644. This peptide has been shown to interact with model membranes and to inhibit viral infectivity. The peptidodendrimer inhibits both HSV-1 and HSV-2 at a very early stage of the entry process, most likely through an interaction with the viral envelope glycoproteins; thus, preventing the virus from coming into close contact with cellular membranes, a prerequisite of viral internalization. The 50% inhibitory concentration was 100 and 300 nM against HSV-1 and HSV-2 respectively, with no evidence of cell toxicity at these concentrations. These results show that the functionalization of a dendrimer with the peptide sequence derived from an HSV glycoprotein shows promising inhibitory activity towards viruses of the Herpesviridae family.Keywords: peptidodendrimer, antiviral activity, membranotropic peptidesTarallo RCarberry TPFalanga AVitiello MGaldiero SGaldiero MWeck MDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2013, Iss default, Pp 521-534 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine (General)
R5-920
spellingShingle Medicine (General)
R5-920
Tarallo R
Carberry TP
Falanga A
Vitiello M
Galdiero S
Galdiero M
Weck M
Dendrimers functionalized with membrane-interacting peptides for viral inhibition
description Rossella Tarallo,1 Tom P Carberry,2 Annarita Falanga,1 Mariateresa Vitiello,3 Stefania Galdiero,1 Massimiliano Galdiero,3 Marcus Weck21Dipartimento di Farmacia, Università di Napoli "Federico II," and DFM Scarl, Napoli, Italia; 2Molecular Design Institute and Department of Chemistry, New York University, New York, NY, USA; 3Dipartimento di Medicina Sperimentale, Seconda Università degli Studi di Napoli, Napoli, ItaliaAbstract: This contribution reports the synthesis of a poly(amide)-based dendrimer functionalized at the termini with a membrane-interacting peptide derived from the herpes simplex virus (HSV) type 1 glycoprotein H, namely gH625-644. This peptide has been shown to interact with model membranes and to inhibit viral infectivity. The peptidodendrimer inhibits both HSV-1 and HSV-2 at a very early stage of the entry process, most likely through an interaction with the viral envelope glycoproteins; thus, preventing the virus from coming into close contact with cellular membranes, a prerequisite of viral internalization. The 50% inhibitory concentration was 100 and 300 nM against HSV-1 and HSV-2 respectively, with no evidence of cell toxicity at these concentrations. These results show that the functionalization of a dendrimer with the peptide sequence derived from an HSV glycoprotein shows promising inhibitory activity towards viruses of the Herpesviridae family.Keywords: peptidodendrimer, antiviral activity, membranotropic peptides
format article
author Tarallo R
Carberry TP
Falanga A
Vitiello M
Galdiero S
Galdiero M
Weck M
author_facet Tarallo R
Carberry TP
Falanga A
Vitiello M
Galdiero S
Galdiero M
Weck M
author_sort Tarallo R
title Dendrimers functionalized with membrane-interacting peptides for viral inhibition
title_short Dendrimers functionalized with membrane-interacting peptides for viral inhibition
title_full Dendrimers functionalized with membrane-interacting peptides for viral inhibition
title_fullStr Dendrimers functionalized with membrane-interacting peptides for viral inhibition
title_full_unstemmed Dendrimers functionalized with membrane-interacting peptides for viral inhibition
title_sort dendrimers functionalized with membrane-interacting peptides for viral inhibition
publisher Dove Medical Press
publishDate 2013
url https://doaj.org/article/56a726a661784ecf8b04be883ec88c0a
work_keys_str_mv AT tarallor dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT carberrytp dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT falangaa dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT vitiellom dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT galdieros dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT galdierom dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
AT weckm dendrimersfunctionalizedwithmembraneinteractingpeptidesforviralinhibition
_version_ 1718401853931126784