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A Surface Plasmon Resonance Analysis of the Interaction between the Antibiotic Moenomycin A and Penicillin‐Binding Protein 1b
Author(s) -
Stembera Katherina,
Vogel Stefan,
Buchynskyy Andrij,
Ayala Juan A.,
Welzel Peter
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020603)3:6<559::aid-cbic559>3.0.co;2-#
Subject(s) - surface plasmon resonance , penicillin , antibiotics , chemistry , resonance (particle physics) , biophysics , microbiology and biotechnology , nuclear magnetic resonance , nanotechnology , biochemistry , materials science , biology , physics , nanoparticle , particle physics
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 in enzymes such as penicillin‐binding protein (PBP) 1b. A novel assay based on surface plasmon resonance (SPR) has been established that can be used to investigate selective binding of the moenomycin sugar moiety and other transglycosylase inhibitors to this enzyme. Suitable ligands were prepared from moenomycin A and coupled to SPR sensor surfaces. Moenomycin analogues with structural variations were used to perform competitive SPR experiments with PBP 1b. The SPR results confirm for the first time that the trisaccharide fragment of moenomycin A (C‐E‐F‐G‐H‐I) is the minimal structure that possesses all moieties sufficient for biological activity and for affinity towards PBP 1b. The method seems to be appropriate for use in screens for transglycosylase inhibitors that bind to the moenomycin‐binding site of the enzyme.