Sugar-lectin interactions investigated through affinity capillary electrophoresis.
The affinity interactions of Concanavalin A (Con A) with various saccharide oligomers (dextrins, dextrans, and selected N-linked glycans from various glycoproteins) have been investigated through a capillary electrophoresis approach. Con A has shown a notable binding discrimination between the alpha-1,6-linked dextran and alpha-1,4-linked dextrin oligomers. Both the binding capacity and binding discrimination appear to decrease with an increase in sugar chainlength. While the core structure of N-linked glycans is deemed to be responsible for the overall binding of various glycans to Con A, the presence of mannose units at the non-reducing ends was found to be very beneficial to the affinity interaction with Con A. Finally, a connection between the glycan-lectin interaction and glycoprotein-lectin interaction has also been suggested.
Department of Chemistry, Indiana University, Bloomington 47405, USA.
M
M
Hong
A
A
Cassely
Y
Y
Mechref
M V
MV
Novotny
D002241:Carbohydrates / Q000737:chemistry*; D003208:Concanavalin A / Q000737:chemistry*; D019075:Electrophoresis, Capillary / Q000379:methods*; D006863:Hydrogen-Ion Concentration
D002241:Carbohydrates; D003208:Concanavalin A