PMID: 11933234Apr 5, 2002Paper

Moenomycin-mediated affinity purification of penicillin-binding protein 1b

Chembiochem : a European Journal of Chemical Biology
Katherina StemberaPeter Welzel

Abstract

The antibiotic moenomycin A inhibits the biosynthesis of peptidoglycan, the main structural polymer of the bacterial cell wall. The inhibition is based on a reversible binding of the antibiotic to one of the substrate binding sites at enzymes such as the penicillin binding protein 1b (PBP 1b). This binding has been employed to isolate PBP 1b by affinity chromatography. Suitable ligands have been prepared from moenomycin A and coupled both to affinity supports and to surface plasmon resonance sensor surfaces. The reactions that take place upon immobilization of the ligands to the affinity support and the sensor surface, respectively, have been studied in detail. With the help of surface plasmon resonance the optimal conditions for binding of PBP 1b to moenomycin-derivated ligands have been established. For the first time the selective binding of the moenomycin sugar moiety to the enzyme has been demonstrated.

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Citations

Jun 6, 2003·Bioorganic & Medicinal Chemistry·Thomas RühlPeter Welzel
Aug 24, 2010·Natural Product Reports·Bohdan Ostash, Suzanne Walker
Apr 26, 2003·Proceedings of the National Academy of Sciences of the United States of America·Lan ChenDaniel Kahne
Jan 21, 2004·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Dec 3, 2014·Biochemical Pharmacology·Daniel BuryMohammed Terrak
May 6, 2006·Medicinal Research Reviews·Masahiko Seki
Oct 5, 2021·Chembiochem : a European Journal of Chemical Biology·Pei-Yu HsiehWei-Chieh Cheng
Sep 27, 2002·Chembiochem : a European Journal of Chemical Biology·Katherina StemberaPeter Welzel

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