A versatile library of activity-based probes for fluorescence detection and/or affinity isolation of lipolytic enzymes

Heidrun Susani-Etzerodt, Hannes Schmidinger, Gernot Riesenhuber , Ruth Birner-Grünberger, Albin Hermetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


This work describes the synthesis of a library of fluorescent and/or biotinylated alkylphosphonate inhibitors being reactive towards serine hydrolases, especially lipases and esterases. Fluorescent inhibitors can be used for sensitive and rapid detection of active proteins by gel electrophoresis. Biotinylated inhibitors are applicable for the enrichment and isolation of active enzymes. Functionality as well as the different detection methods of the synthesized inhibitors were successfully tested with an enzyme preparation, namely cholesterol esterase from porcine pancreas (ppCE). Moreover, a biotinylated inhibitor was employed to enrich ppCE on avidin beads. Hence, our set of phosphonate inhibitors can be used for the detection and/or isolation of active serine hydrolases.
Original languageEnglish
Pages (from-to)60-68
JournalChemistry and Physics of Lipids
Issue number1
Publication statusPublished - 2006

Treatment code (Nähere Zuordnung)

  • Basic - Fundamental (Grundlagenforschung)

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