Use of amoxicillin/sulbactam/trifamox in acute bacterial sinusitis

Abstract

The most common mechanism of bacterial resistance accounting for about 80% of all cases is the enzymatic cleavage of the antibiotic. Enzymes that destroy β-lactam antibiotics are called β-lactamases. They destroy the amide bond in the β-lactam ring of β-lactam antibiotics, which manifests itself as the absence of the result of the action of antibiotics. The use of β-lactamase inhibitors (clavulanic acid, sulbactam and tazobactam) allows maintaining the benefits of long-known efficient antibiotics. Based on the β-lactam structure, they have a high affinity for β-lactamases and, as a result of a complex physicochemical process, form stable inactive complexes with these enzymes (β-lactamases suicide inhibitor). Under the influence of β-lactamases produced by bacteria, they are not hydrolyzed, like amoxicillin, but are firmly bound to them, protecting amoxicillin from hydrolysis. The use of Trifamox in modern antibiotic therapy is relevant not only in the hospital, but also on an outpatient basis, with recurrent diseases that are not amenable to treatment with conventional β-lactams.