Dendrimer functionalization with a membrane-interacting domain of herpes simplex virus type 1: Towards intracellular delivery

Tom P. Carberry, Rossella Tarallo, Annarita Falanga, Emiliana Finamore, Massimiliano Galdiero, Marcus Weck, Stefania Galdiero

Research output: Contribution to journalArticlepeer-review

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 delivery.

Original languageEnglish (US)
Pages (from-to)13678-13685
Number of pages8
JournalChemistry - A European Journal
Volume18
Issue number43
DOIs
StatePublished - Oct 22 2012

Keywords

  • click chemistry
  • delivery
  • dendrimers
  • membrane translocation
  • peptides

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Dendrimer functionalization with a membrane-interacting domain of herpes simplex virus type 1: Towards intracellular delivery'. Together they form a unique fingerprint.

Cite this