Modulating glycosidase degradation and lectin recognition of gold glyconanoparticles.
Glyconanoparticles (GNPs) are water-soluble carbohydrate-functionalized gold nanoclusters with a promising potential to serve as versatile tools in studies ranging from basic chemical glycobiology to clinical applications. In this paper we evaluate the influence of ligand density and presentation on the recognition by protein receptors by examining the interaction of lactose-functionalized GNPs with two different galactose-specific carbohydrate-binding proteins: an enzyme, Escherichia coli beta-galactosidase, and a lectin, Viscum album agglutinin. The results suggest that the proper selection of ligand densities and spacers in GNP functionalization is an important requisite to match the topological requirements of the target receptor while escaping glycosidase degradation.
Barrientos
Africa G
AG
Laboratory of Glyconanotechnology, IIQ-CSIC, Seville, Spain.
de la Fuente
Jesús M
JM
Jiménez
Marta
M
Solís
Dolores
D
Cañada
F Javier
FJ
Martín-Lomas
Manuel
M
Penadés
Soledad
S
D000373:Agglutinins / Q000378:metabolism*; D002240:Carbohydrate Sequence; D029968:Escherichia coli Proteins / Q000378:metabolism; D006046:Gold / Q000737:chemistry*; D053768:Metal Nanoparticles / Q000737:chemistry*; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000378:metabolism*; D011485:Protein Binding; D028182:Viscum album / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism*
D000373:Agglutinins; D029968:Escherichia coli Proteins; D037121:Plant Lectins; D006046:Gold; D001616:beta-Galactosidase