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Dendrimer Functionalization with a Membrane‐Interacting Domain of Herpes Simplex Virus Type 1: Towards Intracellular Delivery
Author(s) -
Carberry Tom P.,
Tarallo Rossella,
Falanga Annarita,
Finamore Emiliana,
Galdiero Massimiliano,
Weck Marcus,
Galdiero Stefania
Publication year - 2012
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201202358
Subject(s) - dendrimer , herpes simplex virus , peptide , surface modification , chemistry , biophysics , viral envelope , membrane , intracellular , drug delivery , conjugate , scaffold , glycoprotein , virus , biochemistry , virology , biology , medicine , mathematical analysis , mathematics , organic chemistry , biomedical engineering
A poly(amide)‐based dendrimer was synthesized and functionalized with the membrane‐interacting peptide gH(625–644) (gH625) derived from the herpes simplex virus type 1 (HSV‐1) envelope glycoprotein H, which has previously been shown to assist in delivering large cargoes across the cellular membrane. We demonstrate that the attachment of the gH625 peptide sequence to the termini of a dendrimer allows the conjugate to penetrate into the cellular matrix, whereas the unfunctionalized dendrimer is excluded from translocation. The peptide‐functionalized dendrimer is rapidly taken into the cells mainly through a non‐active translocation mechanism. Our results suggest that the presented peptidodendrimeric scaffold may be a promising material for efficient drug delivery.