Nonstatistical binding of a protein to clustered carbohydrates.
Carbohydrate-derivatized self-assembled monolayers (SAMs) are used as a model system to address issues involving cell-surface carbohydrate-protein interactions. Here we examine the influence of carbohydrate surface density on protein-binding avidity. We show that the binding selectivity of Bauhinia purpurea lectin switches from one carbohydrate ligand to another as the surface density of the carbohydrate ligands increases from values of chi(sugar) approximately 0.1-1.0. Polyvalent binding is possible at all surface densities investigated; hence, the switch in selectivity is not due simply to the achievement of a critical density that permits polyvalent contacts. Instead, secondary interactions at high surface densities promote a switch in carbohydrate-binding selectivity. These findings may have implications for how changes in the composition and the density of cell-surface carbohydrates influence biological recognition processes and regulatory pathways.
Horan
N
N
Department of Chemistry, Princeton University, Princeton, NJ 08544, USA.
Yan
L
L
Isobe
H
H
Whitesides
G M
GM
Kahne
D
D
D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D002256:Carbonic Anhydrases / Q000378:metabolism; D003208:Concanavalin A / Q000378:metabolism; D017612:Gold Compounds / Q000378:metabolism; D007700:Kinetics; D037102:Lectins / Q000378:metabolism; D008024:Ligands; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D013052:Spectrometry, X-Ray Emission; D020349:Surface Plasmon Resonance
D017612:Gold Compounds; D037102:Lectins; D008024:Ligands; D011506:Proteins; D003208:Concanavalin A; D002256:Carbonic Anhydrases