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

• Published in: PloS one Vol. 9; no. 11; p. e112128
• Main Authors: Falanga, Annarita, Tarallo, Rossella, Carberry, Thomas, Galdiero, Massimiliano, Weck, Marcus, Galdiero, Stefania
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 25.11.2014; Public Library of Science (PLoS)
• Subjects: Biochemistry; Biocompatibility; Biology and Life Sciences; Calorimetry; Dendrimers; Dendrimers - chemistry; Drug delivery; Drug delivery systems; Fluorescence; Fluorescence spectroscopy; Glycoprotein H; Glycoproteins; Herpes simplex; Internalization; Lipids; Liposomes; Liposomes - chemistry; Membranes; Peptides; Peptides - chemistry; Peptides - metabolism; Permeability; Pharmacy; Physical chemistry; Pore formation; Protein Binding; Spectroscopy; Surface plasmon resonance; Titration; Titration calorimetry; Translocation; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - metabolism; Viruses; New York; United States > US; Italy
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0112128

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.