Crystallography and QM/MM Simulations Identify Preferential Binding of Hydrolyzed Carbapenem and Penem Antibiotics to the L1 Metallo-β-Lactamase in the Imine Form.
Sign Up to like & getrecommendations! Published in 2021 at "Journal of chemical information and modeling"
DOI: 10.1021/acs.jcim.1c00663
Abstract: Widespread bacterial resistance to carbapenem antibiotics is an increasing global health concern. Resistance has emerged due to carbapenem-hydrolyzing enzymes, including metallo-β-lactamases (MβLs), but despite their prevalence and clinical importance, MβL mechanisms are still not fully… read more here.
Keywords: hydrolyzed carbapenem; crystallography; penem; different binding ... See more keywords
Structure-Activity Relationship of Penem Antibiotic Side Chains Used against Mycobacteria Reveals Highly Active Compounds.
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DOI: 10.1021/acsinfecdis.2c00229
Abstract: The rise of antibiotic-resistant Mycobacterium tuberculosis and non-tuberculous mycobacterial infections has placed ever-increasing importance on discovering new antibiotics to treat these diseases. Recently, a new penem, T405, was discovered to have strong antimicrobial activity against… read more here.
Keywords: structure activity; side; activity relationship; activity ... See more keywords
Development of a penem antibiotic against Mycobacteroides abscessus
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DOI: 10.1038/s42003-020-01475-2
Abstract: β-lactams are the most widely used antibiotic class to treat bacterial infections in humans. Mycobacteroides abscessus is an emerging pulmonary pathogen resistant to most antibiotics, including penicillins and cephalosporins. With no current FDA-approved treatment and… read more here.
Keywords: development penem; t405; penem antibiotic; mycobacteroides abscessus ... See more keywords