The use of penicillin G, β-lactam-containing antibiotic has began the era of antibacterial therapy. The therapeutic use of penicillin G preserved the millions patients. Thousands of derivatives have been designed around the simple 2-azetidinone ring. Despite discoveries, syntheses and administration of new β-lactam derived and other antibiotics, the war against infectious bacteria continues. Within a short time after introduction of each new antibiotic, nature seems to deliver a counter punch in the form of newly resistant bacteria. Microbes have altered their permeability barriers, drug target binding sites or even induced synthesis of β-lactamases to destroy antibiotics. While continued effort is needed to extend the effectiveness of current antibacterial arsenal and to identify alternate drug targets, innovative approaches to antibacterial treatment are urgently needed.

The previously conducted experiments showed that strain Streptomyces sp. from National Institute of Hygiene Collection is producer of inhibitors of DD-peptidase 64-575 and the inhibition is not degraded by β-lactamases of classes A, B, and C and in wide range of pH. The inhibitor of DD-peptidase was obtained on the way of biosynthesis. Culture of Streptomyces sp. was elaborated by centrifugation to obtain supernatant. Futher steps of purification: acetone protein precipitation, liquid chromatography (anion-exchange, pH gradient ), HPLC (C18 phase). The inhibitor was characterised as follow: physico-chemical properities: the MW of 207.1 was obtained from MS, some structural information (heterocyclic compound, carboxylic group) was obtained with NMR. Inhibitor showed antibacterial activity against Proteus vulgaris and Escherichia coli). Futher experiments will be done to establish the chemical structure of the novel β-lactams (grant MNiE 3 PO5F 033 24).

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