The intriguing journey of gH625-dendrimers

A. Falanga, L. Lombardi, R. Tarallo, G. Franci, E. Perillo, L. Palomba, M. Galdiero, D. Pontoni, G. Fragneto, Marcus Weck, S. Galdiero

Research output: Contribution to journalArticle

Abstract

The knowledge of the mechanism used by vectors to gain access to cell interiors is key to the development of effective drug delivery tools for different pathologies. The role of the initial interaction with the membrane bilayer is widely recognized, although not fully understood. We use neutron reflectivity experiments and internalization studies with cells to reveal the extent of interaction of dendrimers functionalized with the peptide gH625 with biomimetic membranes. We further investigate the internalization by use of Caco-2 cells for assessing the membrane permeability properties of the peptide-dendrimer construct. Neutron reflectivity allowed for the hypothesis that the peptide-dendrimer is able to pass across the bilayer which was confirmed via permeability studies. We find that gH625-dendrimers interact more strongly with cholesterol containing membranes. The advances in our understanding of the mechanism of drug uptake are extremely useful to push further the design of new drug delivery systems.

Original languageEnglish (US)
Pages (from-to)9106-9114
Number of pages9
JournalRSC Advances
Volume7
Issue number15
DOIs
StatePublished - 2017

Fingerprint

Dendrimers
Peptides
Membranes
Neutrons
Cholesterol
Biomimetics
Pathology
Drug delivery
Pharmaceutical Preparations
Experiments

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Falanga, A., Lombardi, L., Tarallo, R., Franci, G., Perillo, E., Palomba, L., ... Galdiero, S. (2017). The intriguing journey of gH625-dendrimers. RSC Advances, 7(15), 9106-9114. https://doi.org/10.1039/c6ra28405a

The intriguing journey of gH625-dendrimers. / Falanga, A.; Lombardi, L.; Tarallo, R.; Franci, G.; Perillo, E.; Palomba, L.; Galdiero, M.; Pontoni, D.; Fragneto, G.; Weck, Marcus; Galdiero, S.

In: RSC Advances, Vol. 7, No. 15, 2017, p. 9106-9114.

Research output: Contribution to journalArticle

Falanga, A, Lombardi, L, Tarallo, R, Franci, G, Perillo, E, Palomba, L, Galdiero, M, Pontoni, D, Fragneto, G, Weck, M & Galdiero, S 2017, 'The intriguing journey of gH625-dendrimers', RSC Advances, vol. 7, no. 15, pp. 9106-9114. https://doi.org/10.1039/c6ra28405a
Falanga A, Lombardi L, Tarallo R, Franci G, Perillo E, Palomba L et al. The intriguing journey of gH625-dendrimers. RSC Advances. 2017;7(15):9106-9114. https://doi.org/10.1039/c6ra28405a
Falanga, A. ; Lombardi, L. ; Tarallo, R. ; Franci, G. ; Perillo, E. ; Palomba, L. ; Galdiero, M. ; Pontoni, D. ; Fragneto, G. ; Weck, Marcus ; Galdiero, S. / The intriguing journey of gH625-dendrimers. In: RSC Advances. 2017 ; Vol. 7, No. 15. pp. 9106-9114.
@article{f891eac0efae45c19ad5c5486a31ca83,
title = "The intriguing journey of gH625-dendrimers",
abstract = "The knowledge of the mechanism used by vectors to gain access to cell interiors is key to the development of effective drug delivery tools for different pathologies. The role of the initial interaction with the membrane bilayer is widely recognized, although not fully understood. We use neutron reflectivity experiments and internalization studies with cells to reveal the extent of interaction of dendrimers functionalized with the peptide gH625 with biomimetic membranes. We further investigate the internalization by use of Caco-2 cells for assessing the membrane permeability properties of the peptide-dendrimer construct. Neutron reflectivity allowed for the hypothesis that the peptide-dendrimer is able to pass across the bilayer which was confirmed via permeability studies. We find that gH625-dendrimers interact more strongly with cholesterol containing membranes. The advances in our understanding of the mechanism of drug uptake are extremely useful to push further the design of new drug delivery systems.",
author = "A. Falanga and L. Lombardi and R. Tarallo and G. Franci and E. Perillo and L. Palomba and M. Galdiero and D. Pontoni and G. Fragneto and Marcus Weck and S. Galdiero",
year = "2017",
doi = "10.1039/c6ra28405a",
language = "English (US)",
volume = "7",
pages = "9106--9114",
journal = "RSC Advances",
issn = "2046-2069",
publisher = "Royal Society of Chemistry",
number = "15",

}

TY - JOUR

T1 - The intriguing journey of gH625-dendrimers

AU - Falanga, A.

AU - Lombardi, L.

AU - Tarallo, R.

AU - Franci, G.

AU - Perillo, E.

AU - Palomba, L.

AU - Galdiero, M.

AU - Pontoni, D.

AU - Fragneto, G.

AU - Weck, Marcus

AU - Galdiero, S.

PY - 2017

Y1 - 2017

N2 - The knowledge of the mechanism used by vectors to gain access to cell interiors is key to the development of effective drug delivery tools for different pathologies. The role of the initial interaction with the membrane bilayer is widely recognized, although not fully understood. We use neutron reflectivity experiments and internalization studies with cells to reveal the extent of interaction of dendrimers functionalized with the peptide gH625 with biomimetic membranes. We further investigate the internalization by use of Caco-2 cells for assessing the membrane permeability properties of the peptide-dendrimer construct. Neutron reflectivity allowed for the hypothesis that the peptide-dendrimer is able to pass across the bilayer which was confirmed via permeability studies. We find that gH625-dendrimers interact more strongly with cholesterol containing membranes. The advances in our understanding of the mechanism of drug uptake are extremely useful to push further the design of new drug delivery systems.

AB - The knowledge of the mechanism used by vectors to gain access to cell interiors is key to the development of effective drug delivery tools for different pathologies. The role of the initial interaction with the membrane bilayer is widely recognized, although not fully understood. We use neutron reflectivity experiments and internalization studies with cells to reveal the extent of interaction of dendrimers functionalized with the peptide gH625 with biomimetic membranes. We further investigate the internalization by use of Caco-2 cells for assessing the membrane permeability properties of the peptide-dendrimer construct. Neutron reflectivity allowed for the hypothesis that the peptide-dendrimer is able to pass across the bilayer which was confirmed via permeability studies. We find that gH625-dendrimers interact more strongly with cholesterol containing membranes. The advances in our understanding of the mechanism of drug uptake are extremely useful to push further the design of new drug delivery systems.

UR - http://www.scopus.com/inward/record.url?scp=85011002348&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85011002348&partnerID=8YFLogxK

U2 - 10.1039/c6ra28405a

DO - 10.1039/c6ra28405a

M3 - Article

AN - SCOPUS:85011002348

VL - 7

SP - 9106

EP - 9114

JO - RSC Advances

JF - RSC Advances

SN - 2046-2069

IS - 15

ER -