Working together with researchers from the United Kingdom and Poland, Professor Dr. Roderich Süssmuth’s Organic and Biological Chemistry Group at TU Berlin has used electron microscopy at low temperatures to create snapshots of how albicidin inhibits a vital enzyme in bacteria. By gaining a detailed understanding of this mechanism of action, they were then able to use computer simulations and chemical synthesis in labs to create variants of the original albicidin molecule that are effective against some of the most dangerous bacterial infections in hospitals. Their findings have now been published in the journal “Nature Catalysis.”
Multi-drug resistant pathogens such as Escherichia coli, Pseudomonas aeruginosa and Salmonella typhimurium represent a dangerous burden for healthcare systems, further exacerbated by the COVID-19 pandemic. Infections with resistant pathogens are one of the most common causes of death in intensive care units, with some strains becoming pan-resistant, meaning that all common antibiotics no longer work. More than 35,000 people die each year in Europe as a result of antibiotic resistances according to the European Centre for Disease Prevention and Control (ECDC). As a result, there is now an urgent search for new antibiotics which are effective against many bacteria and against which resistances cannot be so quickly developed.
Study: Molecular mechanism of topoisomerase poisoning by the peptide antibiotic albicidin