[Affinity of penicillin-binding proteins of Escherichia coli K-12 for furbenicillin and other beta-lactam antibiotics].

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Lei Y, Li JT

[Affinity of penicillin-binding proteins of Escherichia coli K-12 for furbenicillin and other beta-lactam antibiotics].

Zhongguo Yao Li Xue Bao. 1989 Mar;10(2):177-80.

PubMed ID

2683579 [ View in PubMed

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Abstract

Penicillin-binding proteins (PBP) are vitally important targets in relation to the killing of bacteria by beta-lactams. The affinities of PBP of Escherichia coli K 12 for ampicillin, mecillinam and for ureidopenicillins were studied by sodium dodecylsulphate polyacrylamide slab gel electrophoresis and fluorography. The results showed that furbenicillin, a semisynthetic ureidopenicillin developed in China, bound to all 3 essential target proteins of E coli. The IC50 values of furbenicillin to PBP 1 b, PBP 2 and PBP 3 were 4.55 mg/L, 0.37 mg/L and 0.06 mg/L, respectively. The affinities of the 3 proteins of E coli for furbenicillin were 2.5-, 3.5-, and 2.5-fold, respectively higher than that of azlocillin. Mecillinam bound exclusively to PBP 2 (IC50: 0.16 mg/L). Mezlocillin and piperacillin showed higher affinities for PBP 3 than furbenicillin, but their affinities for PBP 1 b and PBP 2 were much lower than furbenicillin.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Mezlocillin	Penicillin-binding protein 1A	Protein	Clostridium perfringens (strain 13 / Type A)	Yes	Inhibitor	Details
Mezlocillin	Penicillin-binding protein 2	Protein	Escherichia coli (strain K12)	Unknown	Inhibitor	Details
Mezlocillin	Penicillin-binding protein 3	Protein	Streptococcus pneumoniae	Yes	Inhibitor	Details