Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

Bacterial beta-lactamases are responsible for resistance to beta-lactams, the most important family of antibiotics. Here, the authors reveal cyclic boronate inhibitors that are active against both serine- and metallo-beta-lactamases and represent a promising strategy for combined antimicrobial treat...

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Autores principales:	Jürgen Brem, Ricky Cain, Samuel Cahill, Michael A. McDonough, Ian J. Clifton, Juan-Carlos Jiménez-Castellanos, Matthew B. Avison, James Spencer, Colin W. G. Fishwick, Christopher J. Schofield
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bb894e352b404c67a6c95bd78e1a12a8
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spelling	oai:doaj.org-article:bb894e352b404c67a6c95bd78e1a12a82021-12-02T15:34:09ZStructural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates10.1038/ncomms124062041-1723https://doaj.org/article/bb894e352b404c67a6c95bd78e1a12a82016-08-01T00:00:00Zhttps://doi.org/10.1038/ncomms12406https://doaj.org/toc/2041-1723Bacterial beta-lactamases are responsible for resistance to beta-lactams, the most important family of antibiotics. Here, the authors reveal cyclic boronate inhibitors that are active against both serine- and metallo-beta-lactamases and represent a promising strategy for combined antimicrobial treatments.Jürgen BremRicky CainSamuel CahillMichael A. McDonoughIan J. CliftonJuan-Carlos Jiménez-CastellanosMatthew B. AvisonJames SpencerColin W. G. FishwickChristopher J. SchofieldNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jürgen Brem Ricky Cain Samuel Cahill Michael A. McDonough Ian J. Clifton Juan-Carlos Jiménez-Castellanos Matthew B. Avison James Spencer Colin W. G. Fishwick Christopher J. Schofield Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
description	Bacterial beta-lactamases are responsible for resistance to beta-lactams, the most important family of antibiotics. Here, the authors reveal cyclic boronate inhibitors that are active against both serine- and metallo-beta-lactamases and represent a promising strategy for combined antimicrobial treatments.
format	article
author	Jürgen Brem Ricky Cain Samuel Cahill Michael A. McDonough Ian J. Clifton Juan-Carlos Jiménez-Castellanos Matthew B. Avison James Spencer Colin W. G. Fishwick Christopher J. Schofield
author_facet	Jürgen Brem Ricky Cain Samuel Cahill Michael A. McDonough Ian J. Clifton Juan-Carlos Jiménez-Castellanos Matthew B. Avison James Spencer Colin W. G. Fishwick Christopher J. Schofield
author_sort	Jürgen Brem
title	Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
title_short	Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
title_full	Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
title_fullStr	Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
title_full_unstemmed	Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
title_sort	structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/bb894e352b404c67a6c95bd78e1a12a8
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Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

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