Mechanistic aspects of the stereospecific interactions of immobilized alpha(1)-acid glycoprotein

The stereospecific interaction of a neutral probe molecule, acetonide, with immobilized alpha (1)-acid glycoprotein (AGP) was investigated. Enantiosel ectivity was found to be influenced by the choice of organic modifier, temp erature, and pH. These parameters could be varied to the extent that a reve rsal of elution order could be induced. Our studies found that the role of hydrogen bonding in the chiral discrimination of acetonide was minimal. An inclusion mechanism is proposed with the investigated parameters affecting the access to the binding sites either through induced conformational chang es or steric hindrance.