Receptor mediated binding of avidin to polymer covered liposomes

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Receptor mediated binding of avidin to polymer covered liposomes. / Kaasgaard, T.; Mouritsen, O. G.; Jørgensen, K.

In: Journal of Liposome Research, Vol. 11, No. 1, 24.05.2001, p. 31-42.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kaasgaard, T, Mouritsen, OG & Jørgensen, K 2001, 'Receptor mediated binding of avidin to polymer covered liposomes', Journal of Liposome Research, vol. 11, no. 1, pp. 31-42. https://doi.org/10.1081/LPR-100103168

APA

Kaasgaard, T., Mouritsen, O. G., & Jørgensen, K. (2001). Receptor mediated binding of avidin to polymer covered liposomes. Journal of Liposome Research, 11(1), 31-42. https://doi.org/10.1081/LPR-100103168

Vancouver

Kaasgaard T, Mouritsen OG, Jørgensen K. Receptor mediated binding of avidin to polymer covered liposomes. Journal of Liposome Research. 2001 May 24;11(1):31-42. https://doi.org/10.1081/LPR-100103168

Author

Kaasgaard, T. ; Mouritsen, O. G. ; Jørgensen, K. / Receptor mediated binding of avidin to polymer covered liposomes. In: Journal of Liposome Research. 2001 ; Vol. 11, No. 1. pp. 31-42.

Bibtex

@article{a29d17948d70412e9aaddbceb7928210,
title = "Receptor mediated binding of avidin to polymer covered liposomes",
abstract = "Fluoresence technique involving a receptor-mediated fluorescence increase of bodipy-labeled avidin upon binding to biotinylated lipids has been used to investigate the steric barrier effect of submicellar concentrations of poly(ethylene glycol)-phospholipids (PE-PEG 2000 and PE-PEG 5000) incorporated into pure DPPC liposomes as well as PE-PEG 5000 incorporated into DPPC liposomes containing 20 mol{\%} cholesterol. It is found that the incorporation of PE-PEG lipopolymers into DPPC lipid bilayers lowers the receptor-mediated adhesion of avidin to the biotinylated liposomes. The most pronounced screening effect is observed at surface densities corresponding to the mushroom conformation of the polymer. Furthermore, the results show that the steric baric effect induced by the surface-grafted polymers becomes stronger when the length of the polymer chain increases. In addition it is found that cholesterol improves the barrier effect of PE-PEG 5000 at low lipopolymer concentrations while no effect is observed at higher concentrations. The results reveal that both the surface density and the polymer length of the PE-PEG lipopolymers play a major role for the accessibility of avidin to biotin surface receptors. However, none of the lipopolymers were capable of completely preventing avidin from reaching the surface bound ligands. Cholesterol only affected the barrier effect at lipopolymer concentrations below the mushroom to brush transition. Consequently, from a steric stabilization viewpoint there is no rationale for incorporating cholesterol into liposomes when the PE-PEG lipopolymer concentration exceeds the mushroom to brush transition. The results presented in this study are of importance in relation to a deeper understanding of the interaction of liposome degrading enzymes and proteins with polymer covered liposomes as well as for the receptor-based targeting and interaction of liposomes with cell surface receptors.",
keywords = "Avidin, Biotin, Cholesterol, Drug targeting, Lipopolymer, PEG-liposomes, Receptor-ligand interaction, Steric stabilization",
author = "T. Kaasgaard and Mouritsen, {O. G.} and K. J{\o}rgensen",
year = "2001",
month = "5",
day = "24",
doi = "10.1081/LPR-100103168",
language = "English",
volume = "11",
pages = "31--42",
journal = "Journal of Liposome Research",
issn = "0898-2104",
publisher = "Taylor & Francis",
number = "1",

}

RIS

TY - JOUR

T1 - Receptor mediated binding of avidin to polymer covered liposomes

AU - Kaasgaard, T.

AU - Mouritsen, O. G.

AU - Jørgensen, K.

PY - 2001/5/24

Y1 - 2001/5/24

N2 - Fluoresence technique involving a receptor-mediated fluorescence increase of bodipy-labeled avidin upon binding to biotinylated lipids has been used to investigate the steric barrier effect of submicellar concentrations of poly(ethylene glycol)-phospholipids (PE-PEG 2000 and PE-PEG 5000) incorporated into pure DPPC liposomes as well as PE-PEG 5000 incorporated into DPPC liposomes containing 20 mol% cholesterol. It is found that the incorporation of PE-PEG lipopolymers into DPPC lipid bilayers lowers the receptor-mediated adhesion of avidin to the biotinylated liposomes. The most pronounced screening effect is observed at surface densities corresponding to the mushroom conformation of the polymer. Furthermore, the results show that the steric baric effect induced by the surface-grafted polymers becomes stronger when the length of the polymer chain increases. In addition it is found that cholesterol improves the barrier effect of PE-PEG 5000 at low lipopolymer concentrations while no effect is observed at higher concentrations. The results reveal that both the surface density and the polymer length of the PE-PEG lipopolymers play a major role for the accessibility of avidin to biotin surface receptors. However, none of the lipopolymers were capable of completely preventing avidin from reaching the surface bound ligands. Cholesterol only affected the barrier effect at lipopolymer concentrations below the mushroom to brush transition. Consequently, from a steric stabilization viewpoint there is no rationale for incorporating cholesterol into liposomes when the PE-PEG lipopolymer concentration exceeds the mushroom to brush transition. The results presented in this study are of importance in relation to a deeper understanding of the interaction of liposome degrading enzymes and proteins with polymer covered liposomes as well as for the receptor-based targeting and interaction of liposomes with cell surface receptors.

AB - Fluoresence technique involving a receptor-mediated fluorescence increase of bodipy-labeled avidin upon binding to biotinylated lipids has been used to investigate the steric barrier effect of submicellar concentrations of poly(ethylene glycol)-phospholipids (PE-PEG 2000 and PE-PEG 5000) incorporated into pure DPPC liposomes as well as PE-PEG 5000 incorporated into DPPC liposomes containing 20 mol% cholesterol. It is found that the incorporation of PE-PEG lipopolymers into DPPC lipid bilayers lowers the receptor-mediated adhesion of avidin to the biotinylated liposomes. The most pronounced screening effect is observed at surface densities corresponding to the mushroom conformation of the polymer. Furthermore, the results show that the steric baric effect induced by the surface-grafted polymers becomes stronger when the length of the polymer chain increases. In addition it is found that cholesterol improves the barrier effect of PE-PEG 5000 at low lipopolymer concentrations while no effect is observed at higher concentrations. The results reveal that both the surface density and the polymer length of the PE-PEG lipopolymers play a major role for the accessibility of avidin to biotin surface receptors. However, none of the lipopolymers were capable of completely preventing avidin from reaching the surface bound ligands. Cholesterol only affected the barrier effect at lipopolymer concentrations below the mushroom to brush transition. Consequently, from a steric stabilization viewpoint there is no rationale for incorporating cholesterol into liposomes when the PE-PEG lipopolymer concentration exceeds the mushroom to brush transition. The results presented in this study are of importance in relation to a deeper understanding of the interaction of liposome degrading enzymes and proteins with polymer covered liposomes as well as for the receptor-based targeting and interaction of liposomes with cell surface receptors.

KW - Avidin

KW - Biotin

KW - Cholesterol

KW - Drug targeting

KW - Lipopolymer

KW - PEG-liposomes

KW - Receptor-ligand interaction

KW - Steric stabilization

UR - http://www.scopus.com/inward/record.url?scp=0035026374&partnerID=8YFLogxK

U2 - 10.1081/LPR-100103168

DO - 10.1081/LPR-100103168

M3 - Journal article

AN - SCOPUS:0035026374

VL - 11

SP - 31

EP - 42

JO - Journal of Liposome Research

JF - Journal of Liposome Research

SN - 0898-2104

IS - 1

ER -

ID: 236897042