Polystyrene microbridges used in sitting-drop crystallization release 1,4-diphenyl-2-butene, a novel inhibitor of human MAO B

Frantisek Hubálek, Claudia Binda, Min Li, Andrea Mattevi, Dale E. Edmondson

Research output: Contribution to journalArticlepeer-review

Abstract

In the course of protein-structure determinations of the membrane-bound enzyme monoamine oxidase B (MAO B) by X-ray crystallography, a compound was found in the active site of the enzyme that consists of two phenyl rings separated by four C atoms. This compound was identified by chromatography and by mass spectrometry to be 1,4-diphenyl-2-butene and found to be a component of the polystyrene microbridges that are used in protein crystallization. This compound is present at a level of ∼0.3 mg (∼1.5 μmol) per microbridge and functions as a competitive inhibitor of MAO B with a K i of 35 μM. The presence of detergents in the crystallization solutions facilitates the extraction of this compound from the polymer medium.

Original languageEnglish (US)
Pages (from-to)1874-1876
Number of pages3
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number10
DOIs
StatePublished - Oct 1 2003

ASJC Scopus subject areas

  • Structural Biology

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