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Updated: Feb 2, 2026

Sheathless Capillary Electrophoresis–Mass Spectrometry for Metabolic Profiling of Biological Samples
Published on: October 1, 2016
Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity
Umut Salgin Goksen1,2, Sevgi Sarigul3, Patrick Bultinck4
1Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Hacettepe University, Ankara, Turkey.
Abstract:
A new racemic pyrazoline derivative was synthesized and resolved to its enantiomers using analytic and semipreparative high-pressure liquid chromatography. The absolute configuration of both fractions was established using vibrational circular dichroism. The in vitro monoamine oxidase (MAO) inhibitory profiles were evaluated for the racemate and both enantiomers separately for the two isoforms of the enzyme. The racemic compound and both enantiomers were found to inhibit hMAO-A selectively and competitively. In particular, the R enantiomer was detected as an exceptionally potent and a selective MAO-A inhibitor (Ki = 0.85 × 10-3 ± 0.05 × 10-3 μM and SI: 2.35 × 10-5 ), whereas S was determined as poorer compound than R in terms of Ki and SI (0.184 ± 0.007 and 0.001). The selectivity of the enantiomers was explained by molecular modeling docking studies based on the PDB enzymatic models of MAO isoforms.
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