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Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_uu_465165

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors

About this item

Full title

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors

Publisher

London: Nature Publishing Group UK

Journal title

Nature chemistry, 2022-01, Vol.14 (1), p.15-24

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Carbapenems are vital antibiotics, but their efficacy is increasingly compromised by metallo-β-lactamases (MBLs). Here we report the discovery and optimization of potent broad-spectrum MBL inhibitors. A high-throughput screen for NDM-1 inhibitors identified indole-2-carboxylates (InCs) as potential β-lactamase stable β-lactam mimics. Subsequent str...

Alternative Titles

Full title

Imitation of β-lactam binding enables broad-spectrum metallo-β-lactamase inhibitors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_DiVA_org_uu_465165

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_uu_465165

Other Identifiers

ISSN

1755-4330,1755-4349

E-ISSN

1755-4349

DOI

10.1038/s41557-021-00831-x

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