Mechanistic aspects of the stereospecific interactions of immobilized α1-acid glycoprotein

The stereospecific interaction of a neutral probe molecule, acetonide, with immobilized alpha (1)-acid glycoprotein (AGP) was investigated. Enantioselectivity was found to be influenced by the choice of organic modifier, temperature, and pH. These parameters could be varied to the extent that a reversal 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 changes or steric hindrance.