Amphiphilic alpha-cyclodextrins have been synthesized bearing hexylthio, dodecylthio, and hexadecylthio chains at the 6-positions and glycosylthiocarbamoyl-oligo(ethylene glycol) units at the 2-positions. The glycosyl residues (alpha-D-mannosyl and beta-L-fucosyl) are intended for cell-targeting. Self-assembly of these new amphiphilic glycosylated cyclodextrins in water to form vesicles was investigated by dynamic light scattering and transmission electron microscopy. Selective binding of the hexylthio assemblies to a protein receptor (Lens culinaris lectin) was confirmed by fluorescence spectroscopy.
Amphiphilic N-glycosyl-thiocarbamoyl cyclodextrins: synthesis, selfassembly and fluorimetry of recognition by Lens culinaris lectin / S. McNicholas, A. Rencurosi, L. Lay, A. Mazzaglia, L. Sturiale, M. Perez, R. Darcy. - In: BIOMACROMOLECULES. - ISSN 1525-7797. - 8:6(2007), pp. 1851-1857.
Amphiphilic N-glycosyl-thiocarbamoyl cyclodextrins: synthesis, selfassembly and fluorimetry of recognition by Lens culinaris lectin.
L. Lay;
2007
Abstract
Amphiphilic alpha-cyclodextrins have been synthesized bearing hexylthio, dodecylthio, and hexadecylthio chains at the 6-positions and glycosylthiocarbamoyl-oligo(ethylene glycol) units at the 2-positions. The glycosyl residues (alpha-D-mannosyl and beta-L-fucosyl) are intended for cell-targeting. Self-assembly of these new amphiphilic glycosylated cyclodextrins in water to form vesicles was investigated by dynamic light scattering and transmission electron microscopy. Selective binding of the hexylthio assemblies to a protein receptor (Lens culinaris lectin) was confirmed by fluorescence spectroscopy.
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