Penicillin G acylase as chiral selector in LC and CE: exploring the origins of enantioselectivity.
The review examines the most recent achievement of immobilized Penicillin G acylase (PGA) as chiral stationary phases (PGA-CSP) for the separation of acidic enantiomers. Particular attention is paid to the influence of structural variations of a large number of analytes on retention and enantioselectivity with a special emphasis on advances in the elucidation of the chiral recognition mechanism. Docking calculations and molecular dynamic simulations are discussed to rationalize the origins of enantioselective behaviour. The review also touches the chiral behaviour of PGA in partial filling CE. The CE results, obtained using PGA in free solution, suggest that the immobilization procedure used in the development of PGA-CSPs did not alter the enantioselective properties of the enzyme.
Massolini
G
G
Department of Pharmaceutical Chemistry, University of Pavia, Via Taramelli 12, 27100 Pavia, Italy. g.massolini@unipv.it
Temporini
C
C
Calleri
E
E
D001665:Binding Sites; D002853:Chromatography, Liquid / Q000379:methods*; D003198:Computer Simulation; D019075:Electrophoresis, Capillary / Q000379:methods*; D010399:Penicillin Amidase / Q000737:chemistry*; D010648:Phenylacetates / Q000737:chemistry; D013237:Stereoisomerism
D010648:Phenylacetates; D010399:Penicillin Amidase