β-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

β-Cyclodextrin-appended giant amphiphile : Aggregation to vesicle polymersomes and immobilisation of enzymes. / Felici, Marco; Marzá-Pérez, María; Hatzakis, Nikos S.; Nolte, Roeland J.M.; Feiters, Martin C.

I: Chemistry - A European Journal, Bind 14, Nr. 32, 2008, s. 9914-9920.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Felici, M, Marzá-Pérez, M, Hatzakis, NS, Nolte, RJM & Feiters, MC 2008, 'β-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes', Chemistry - A European Journal, bind 14, nr. 32, s. 9914-9920. https://doi.org/10.1002/chem.200801429

APA

Felici, M., Marzá-Pérez, M., Hatzakis, N. S., Nolte, R. J. M., & Feiters, M. C. (2008). β-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes. Chemistry - A European Journal, 14(32), 9914-9920. https://doi.org/10.1002/chem.200801429

Vancouver

Felici M, Marzá-Pérez M, Hatzakis NS, Nolte RJM, Feiters MC. β-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes. Chemistry - A European Journal. 2008;14(32):9914-9920. https://doi.org/10.1002/chem.200801429

Author

Felici, Marco ; Marzá-Pérez, María ; Hatzakis, Nikos S. ; Nolte, Roeland J.M. ; Feiters, Martin C. / β-Cyclodextrin-appended giant amphiphile : Aggregation to vesicle polymersomes and immobilisation of enzymes. I: Chemistry - A European Journal. 2008 ; Bind 14, Nr. 32. s. 9914-9920.

Bibtex

@article{0c47b85531e9401e90949b9c0a2c0235,
title = "β-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes",
abstract = "A giant amphiphile consisting of polystyrene end-capped with permethylated {\ss}-cyclodextrin was synthesised and found to form vesicular structures when injected as a solution in THF into water. The ability of the cyclodextrins on the surface of the polymersomes to form inclusion complexes with hydrophobic compounds was tested by carrying out a competition experiment with a fluorescent probe sensitive to the polarity of the surrounding medium. It was found that 1-adamantol can displace the fluorescent probe from the cavities of the cyclodextrin moieties of the polymersomes. The recognition of molecules by cell membranes in nature is often based on interactions with specific membrane receptors. To mimic this behaviour, the enzyme horseradish peroxidase was modified with adamantane groups through a poly(ethylene glycol) spacer and its interaction with the polymersomes was investigated. It was established that the presence of adamantane moieties on each enzyme allowed a host-guest interaction with the multifunctional surface of the polymersomes.",
keywords = "Amphiphiles, Click reaction, Cyclodextrins, Enzyme immobilization, Polymersomes",
author = "Marco Felici and Mar{\'i}a Marz{\'a}-P{\'e}rez and Hatzakis, {Nikos S.} and Nolte, {Roeland J.M.} and Feiters, {Martin C.}",
year = "2008",
doi = "10.1002/chem.200801429",
language = "English",
volume = "14",
pages = "9914--9920",
journal = "Chemistry: A European Journal",
issn = "0947-6539",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "32",

}

RIS

TY - JOUR

T1 - β-Cyclodextrin-appended giant amphiphile

T2 - Aggregation to vesicle polymersomes and immobilisation of enzymes

AU - Felici, Marco

AU - Marzá-Pérez, María

AU - Hatzakis, Nikos S.

AU - Nolte, Roeland J.M.

AU - Feiters, Martin C.

PY - 2008

Y1 - 2008

N2 - A giant amphiphile consisting of polystyrene end-capped with permethylated ß-cyclodextrin was synthesised and found to form vesicular structures when injected as a solution in THF into water. The ability of the cyclodextrins on the surface of the polymersomes to form inclusion complexes with hydrophobic compounds was tested by carrying out a competition experiment with a fluorescent probe sensitive to the polarity of the surrounding medium. It was found that 1-adamantol can displace the fluorescent probe from the cavities of the cyclodextrin moieties of the polymersomes. The recognition of molecules by cell membranes in nature is often based on interactions with specific membrane receptors. To mimic this behaviour, the enzyme horseradish peroxidase was modified with adamantane groups through a poly(ethylene glycol) spacer and its interaction with the polymersomes was investigated. It was established that the presence of adamantane moieties on each enzyme allowed a host-guest interaction with the multifunctional surface of the polymersomes.

AB - A giant amphiphile consisting of polystyrene end-capped with permethylated ß-cyclodextrin was synthesised and found to form vesicular structures when injected as a solution in THF into water. The ability of the cyclodextrins on the surface of the polymersomes to form inclusion complexes with hydrophobic compounds was tested by carrying out a competition experiment with a fluorescent probe sensitive to the polarity of the surrounding medium. It was found that 1-adamantol can displace the fluorescent probe from the cavities of the cyclodextrin moieties of the polymersomes. The recognition of molecules by cell membranes in nature is often based on interactions with specific membrane receptors. To mimic this behaviour, the enzyme horseradish peroxidase was modified with adamantane groups through a poly(ethylene glycol) spacer and its interaction with the polymersomes was investigated. It was established that the presence of adamantane moieties on each enzyme allowed a host-guest interaction with the multifunctional surface of the polymersomes.

KW - Amphiphiles

KW - Click reaction

KW - Cyclodextrins

KW - Enzyme immobilization

KW - Polymersomes

U2 - 10.1002/chem.200801429

DO - 10.1002/chem.200801429

M3 - Journal article

C2 - 18810732

AN - SCOPUS:55449101108

VL - 14

SP - 9914

EP - 9920

JO - Chemistry: A European Journal

JF - Chemistry: A European Journal

SN - 0947-6539

IS - 32

ER -

ID: 286411834