| Literature DB >> 32886509 |
Lucy Lin, Margaret E Olson, Takashi Sugane, Lewis D Turner, Margarita A Tararina1, Alexander L Nielsen, Elbek K Kurbanov2, Sabine Pellett3, Eric A Johnson3, Seth M Cohen2, Karen N Allen4, Kim D Janda.
Abstract
Botulinum neurotoxins have remarkable persistence (∼weeks to months in cells), outlasting the small-molecule inhibitors designed to target them. To address this disconnect, inhibitors bearing two pharmacophores-a zinc binding group and a Cys-reactive warhead-were designed to leverage both affinity and reactivity. A series of first-generation bifunctional inhibitors was achieved through structure-based inhibitor design. Through X-ray crystallography, engagement of both the catalytic Zn2+ and Cys165 was confirmed. A second-generation series improved on affinity by incorporating known reversible inhibitor pharmacophores; the mechanism was confirmed by exhaustive dialysis, mass spectrometry, and in vitro evaluation against the C165S mutant. Finally, a third-generation inhibitor was shown to have good cellular activity and low toxicity. In addition to our findings, an alternative method of modeling time-dependent inhibition that simplifies assay setup and allows comparison of inhibition models is discussed.Entities:
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Year: 2020 PMID: 32886509 PMCID: PMC7581224 DOI: 10.1021/acs.jmedchem.0c01006
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446