Structural highlights
Function
[BLAN1_KLEPN] Confers resistance to many beta-lactam antibiotics, including some carbapenems. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin.
Publication Abstract from PubMed
Recent decades have witnessed a dramatic increase of multidrug resistant (MDR) bacteria, compromising the efficacy of available antibiotics, and a continual decline in the discovery of novel antibacterials. We recently reported the first library of benzo[b]thiophen-2-ylboronic acid inhibitors sharing broad spectrum activity against beta-lactamases (BLs). The ability of these compounds to inhibit structurally and mechanistically different types of beta-lactamases has been here structurally investigated. An extensive X-ray crystallographic analysis of boronic acids (BAs) binding to proteins representative of serine BLs (SBLs) and metallo beta-lactamases (MBLs) have been conducted to depict the role played by the boronic group in driving molecular recognition, especially in the interaction with MBLs. Our derivatives are the first case of noncyclic boronic acids active against MBLs and represent a productive route toward potent broad-spectrum inhibitors.
X-ray Crystallography Deciphers the Activity of Broad-Spectrum Boronic Acid beta-Lactamase Inhibitors.,Cendron L, Quotadamo A, Maso L, Bellio P, Montanari M, Celenza G, Venturelli A, Costi MP, Tondi D ACS Med Chem Lett. 2019 Mar 27;10(4):650-655. doi:, 10.1021/acsmedchemlett.8b00607. eCollection 2019 Apr 11. PMID:30996812[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cendron L, Quotadamo A, Maso L, Bellio P, Montanari M, Celenza G, Venturelli A, Costi MP, Tondi D. X-ray Crystallography Deciphers the Activity of Broad-Spectrum Boronic Acid beta-Lactamase Inhibitors. ACS Med Chem Lett. 2019 Mar 27;10(4):650-655. doi:, 10.1021/acsmedchemlett.8b00607. eCollection 2019 Apr 11. PMID:30996812 doi:http://dx.doi.org/10.1021/acsmedchemlett.8b00607
