Elucidation of the interaction mechanism with liposomes of gH625-peptide functionalized dendrimers

Annarita Falanga, Rossella Tarallo, Thomas Carberry, Massimiliano Galdiero, Marcus Weck, Stefania Galdiero

Research output: Contribution to journalArticle

Abstract

We have demonstrated that amide-based dendrimers functionalized with the membrane-interacting peptide gH625 derived from the herpes simplex virus type 1 (HSV-1) envelope glycoprotein H enter cells mainly through a non-active translocation mechanism. Herein, we investigate the interaction between the peptide-functionalized dendrimer and liposomes composed of PC/Chol using fluorescence spectroscopy, isothermal titration calorimetry, and surface plasmon resonance to get insights into the mechanism of internalization. The affinity for the membrane bilayer is very high and the interaction between the peptide-dendrimer and liposomes took place without evidence of pore formation. These results suggest that the presented peptidodendrimeric scaffold may be a promising material for efficient drug delivery.

Original languageEnglish (US)
Article numbere112128
JournalPloS one
Volume9
Issue number11
DOIs
StatePublished - Nov 25 2014

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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