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
Dendrimer Functionalization with a Membrane-Interacting Domain of Herpes Simplex Virus Type 1: Towards Intracellular Delivery
GALDIERO, Massimiliano;
2012
Abstract
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 deliveryI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
