Resumo

URBINA-DAZA, Adrian et al. Theoretical study of compounds derived from cephalosporins with inhibitory activity potential front to penicillin binding proteins (PBP) and resistance to Extended spectrum Beta-lactamase (ESBL) produced by Escherichia coli. Rev. colomb. cienc. quim. farm. [online]. 2019, vol.48, n.1, pp.44-60. ISSN 0034-7418.  https://doi.org/10.15446/rcciquifa.v48n1.80064.

Computational tools have been used to propose molecules derived from cephalosporins with potential antibacterial activity, against strains of Escherichia Coli, with higher affinity as inhibitors of penicillin-binding enzymes and which in turn decrease or do not have affinity for extended-spectrum beta-lactamases. 20 molecules were designed based on the molecular structure of the cephalosporin, the structures were optimized using the density functional theory, molecular descriptors of reactivity were calculated, and in parallel form they were subjected to molecular docking with the enzymes mentioned above. The molecules showed negative binding energy values, 12 molecules showed an orientation and favorable interactions in the active site of the penicillin binding enzyme and thirteen molecules had lower affinity than the native ligand (Cefotaxime) for betalactamase. Three molecules can be considered as potential inhibitors of binding enzymes to resistant penicillins and betalactamases.

Palavras-chave : Cephalosporins; penicillin binding protein; extended-spectrum beta-lactamases; molecular docking.

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