Mode of action: interaction with the penicillin binding proteins

摘要: The introduction of penicillins as antibacterial agents fifty years aga was one the major breakthroughs in chemotherapy. heroic efforts Oxford group to prepare and elucidate structure these molecules paved way for a tremendous number research projects designed understand their mode action, obtain new compounds exhibiting similar properties capable circumventing different resistance mechanisms used by bacteria escape lethai effects. These latter studies resulted synthesis or isolation, from natural sources, large molecules; became more original penicillins, giving rise vast family chemicals whose sole common structural feature four-membered β-lactam ring (see Editorial Introduction, Figure 1). Recently, non-β-lactam structures that appear inactivate β-lactam-specific targets have been described. are members β-lactam-recognizing pro teins , which comprises β-lactamases penicillin binding proteins (PBPs). hydrolyse amide bond represent most efficient mechanism currently responsible bacterial phenomena. PBPs form rather stable covalent adducts with β-lactams. When inactivation results cell death, PBP is considered ‘essential’. In cases, physiological function nonessential remains mysterious