The dendrimer impact on vesicles can be tuned based on the lipid bilayer charge and the presence of albumin

Francesca Ruggeri; Anna Karin Louise Åkesson; Pierre-Yves Chapuis; Catherine Anne Skrzynski Nielsen; Thomas Günther-Pomorski; Marco P. Monopoli; Kenneth A. Dawson; Thomas Günther-Pomorski; Marite Cardenas Gomez

doi:10.1039/C3SM50603G

The dendrimer impact on vesicles can be tuned based on the lipid bilayer charge and the presence of albumin

Francesca Ruggeri, Anna Karin Louise Åkesson, Pierre-Yves Chapuis, Catherine Anne Skrzynski Nielsen, Thomas Günther-Pomorski, Marco P. Monopoli, Kenneth A. Dawson, Thomas Günther-Pomorski, Marite Cardenas Gomez

18 Citations (Scopus)

Abstract

PAMAM (polyamidoamine) dendrimers are promising polymers in biomedical applications that can interact with both the lipid bilayer and proteins. Here we employed giant unilamellar vesicles (GUVs) of two different charge densities to study the effect of albumin, one of the major proteins in blood plasma, on the interactions between PAMAM dendrimers and lipid membranes. The results show that albumin exacerbates the effect of dendrimers on the destabilization of the vesicles in terms of leakage, aggregation and collapse in particular for negatively charged vesicles while neutrally charged membranes are not affected. We conclude that the higher affinity of both albumin and PAMAM G6 towards negatively charged membranes explains their synergistic behavior in this case. In the case of neutral vesicles, the affinity between PAMAM G6 and albumin is stronger than that between PAMAM G6 (or albumin) and neutral vesicles, and thus no synergism is observed for the mixture during the interaction with neutral membranes.

Original language	English
Journal	Soft Matter
Volume	9
Issue number	37
Pages (from-to)	8862-8870
Number of pages	9
ISSN	1744-683X
DOIs	https://doi.org/10.1039/C3SM50603G
Publication status	Published - 7 Oct 2013

Access to Document

10.1039/C3SM50603G

Cite this

@article{086ce64d51c34b6487200efc683c6373,

title = "The dendrimer impact on vesicles can be tuned based on the lipid bilayer charge and the presence of albumin",

abstract = "PAMAM (polyamidoamine) dendrimers are promising polymers in biomedical applications that can interact with both the lipid bilayer and proteins. Here we employed giant unilamellar vesicles (GUVs) of two different charge densities to study the effect of albumin, one of the major proteins in blood plasma, on the interactions between PAMAM dendrimers and lipid membranes. The results show that albumin exacerbates the effect of dendrimers on the destabilization of the vesicles in terms of leakage, aggregation and collapse in particular for negatively charged vesicles while neutrally charged membranes are not affected. We conclude that the higher affinity of both albumin and PAMAM G6 towards negatively charged membranes explains their synergistic behavior in this case. In the case of neutral vesicles, the affinity between PAMAM G6 and albumin is stronger than that between PAMAM G6 (or albumin) and neutral vesicles, and thus no synergism is observed for the mixture during the interaction with neutral membranes.",

author = "Francesca Ruggeri and {\AA}kesson, {Anna Karin Louise} and Pierre-Yves Chapuis and Nielsen, {Catherine Anne Skrzynski} and Thomas G{\"u}nther-Pomorski and Monopoli, {Marco P.} and Dawson, {Kenneth A.} and Thomas G{\"u}nther-Pomorski and {Cardenas Gomez}, Marite",

year = "2013",

month = oct,

day = "7",

doi = "10.1039/C3SM50603G",

language = "English",

volume = "9",

pages = "8862--8870",

journal = "Journal of Materials Chemistry",

issn = "0959-9428",

publisher = "Royal Society of Chemistry",

number = "37",

}

TY - JOUR

T1 - The dendrimer impact on vesicles can be tuned based on the lipid bilayer charge and the presence of albumin

AU - Ruggeri, Francesca

AU - Åkesson, Anna Karin Louise

AU - Chapuis, Pierre-Yves

AU - Nielsen, Catherine Anne Skrzynski

AU - Günther-Pomorski, Thomas

AU - Monopoli, Marco P.

AU - Dawson, Kenneth A.

AU - Günther-Pomorski, Thomas

AU - Cardenas Gomez, Marite

PY - 2013/10/7

Y1 - 2013/10/7

N2 - PAMAM (polyamidoamine) dendrimers are promising polymers in biomedical applications that can interact with both the lipid bilayer and proteins. Here we employed giant unilamellar vesicles (GUVs) of two different charge densities to study the effect of albumin, one of the major proteins in blood plasma, on the interactions between PAMAM dendrimers and lipid membranes. The results show that albumin exacerbates the effect of dendrimers on the destabilization of the vesicles in terms of leakage, aggregation and collapse in particular for negatively charged vesicles while neutrally charged membranes are not affected. We conclude that the higher affinity of both albumin and PAMAM G6 towards negatively charged membranes explains their synergistic behavior in this case. In the case of neutral vesicles, the affinity between PAMAM G6 and albumin is stronger than that between PAMAM G6 (or albumin) and neutral vesicles, and thus no synergism is observed for the mixture during the interaction with neutral membranes.

AB - PAMAM (polyamidoamine) dendrimers are promising polymers in biomedical applications that can interact with both the lipid bilayer and proteins. Here we employed giant unilamellar vesicles (GUVs) of two different charge densities to study the effect of albumin, one of the major proteins in blood plasma, on the interactions between PAMAM dendrimers and lipid membranes. The results show that albumin exacerbates the effect of dendrimers on the destabilization of the vesicles in terms of leakage, aggregation and collapse in particular for negatively charged vesicles while neutrally charged membranes are not affected. We conclude that the higher affinity of both albumin and PAMAM G6 towards negatively charged membranes explains their synergistic behavior in this case. In the case of neutral vesicles, the affinity between PAMAM G6 and albumin is stronger than that between PAMAM G6 (or albumin) and neutral vesicles, and thus no synergism is observed for the mixture during the interaction with neutral membranes.

U2 - 10.1039/C3SM50603G

DO - 10.1039/C3SM50603G

M3 - Journal article

SN - 0959-9428

VL - 9

SP - 8862

EP - 8870

JO - Journal of Materials Chemistry

JF - Journal of Materials Chemistry

IS - 37

ER -

The dendrimer impact on vesicles can be tuned based on the lipid bilayer charge and the presence of albumin

Abstract

Access to Document

Fingerprint

Cite this