Side chain SAR of bicyclic β-lactamase inhibitors (BLIs). 2. N-Alkylated and open chain analogs of MK-8712

Autor:	Douglas Wisniewski, Nichelle Hairston, Seongkon Kim, Timothy A. Blizzard, Aimie M. Ogawa, Jane Y. Wu, Young-Whan Park, Milton L. Hammond, Ronald E. Painter, Katherine Young, Jeff Hermes, Susan L. Raghoobar, Giovanna Scapin, Nandini Sharma, Helen Chen, Paula M.D. Fitzgerald, Jun Lu
Rok vydání:	2011
Předmět:	Imipenem Molecular model Stereochemistry Clinical Biochemistry Pharmaceutical Science Microbial Sensitivity Tests Biochemistry beta-Lactamases Structure-Activity Relationship Drug Discovery polycyclic compounds medicine Side chain Monobactam Computer Simulation Enzyme Inhibitors Molecular Biology Antibacterial agent chemistry.chemical_classification Binding Sites Bicyclic molecule biology Organic Chemistry biochemical phenomena metabolism and nutrition bacterial infections and mycoses Anti-Bacterial Agents Protein Structure Tertiary Enzyme chemistry Enzyme inhibitor biology.protein Molecular Medicine beta-Lactamase Inhibitors medicine.drug Monobactams
Zdroj:	Bioorganicmedicinal chemistry letters. 21(14)
ISSN:	1464-3405
Popis:	The bridged monobactam β-lactamase inhibitor MK-8712 (1) effectively inhibits class C β-lactamases. Side chain N-alkylated and ring-opened analogs of 1 were prepared and evaluated for combination with imipenem to overcome class C β-lactamase mediated resistance. Although some analogs were more potent inhibitors of AmpC, none exhibited better synergy with imipenem than 1.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af0c4138f7c39ede92a29f86721a221d https://pubmed.ncbi.nlm.nih.gov/21676616 Zobrazit plný text záznamu Full Text from ScienceDirect