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Moenomycin‐Mediated Affinity Purification of Penicillin‐Binding Protein 1b
Author(s) -
Stembera Katherina,
Buchynskyy Andrij,
Vogel Stefan,
Knoll Dietmar,
Osman Awad A.,
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(20020402)3:4<332::aid-cbic332>3.0.co;2-b
Subject(s) - surface plasmon resonance , penicillin binding proteins , affinity chromatography , moiety , peptidoglycan , chemistry , enzyme , substrate (aquarium) , biochemistry , binding site , stereochemistry , combinatorial chemistry , penicillin , biology , antibiotics , materials science , nanotechnology , ecology , nanoparticle
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.