Stimuli-responsive receptors for the recognition unit of the cholera toxin (CTB) have been prepared by attaching
multiple copies of its natural carbohydrate ligand, the GM1 oligosaccharide, to a thermoresponsive polymer scaffold. Below their
lower critical solution temperature (LCST), polymers complex CTB with nanomolar affinity. When heated above their LCST,
polymers undergo a reversible coil to globule transition which renders a proportion of the carbohydrate recognition motifs
inaccessible to CTB. This thermally-modulated decrease in the avidity of the material for the protein has been used to reversibly
capture CTB from solution, enabling its convenient isolation from a complex mixture.
Stimuli-responsive receptors for the recognition unit of the cholera toxin (CTB) have been prepared by attaching
multiple copies of its natural carbohydrate ligand, the GM1 oligosaccharide, to a thermoresponsive polymer scaffold. Below their
lower critical solution temperature (LCST), polymers complex CTB with nanomolar affinity. When heated above their LCST,
polymers undergo a reversible coil to globule transition which renders a proportion of the carbohydrate recognition motifs
inaccessible to CTB. This thermally-modulated decrease in the avidity of the material for the protein has been used to reversibly
capture CTB from solution, enabling its convenient isolation from a complex mixture.
