| Literature DB >> 29198864 |
Guan-Sheng Jiao1, Seongjin Kim1, Mahtab Moayeri2, April Thai1, Lynne Cregar-Hernandez1, Linda McKasson1, Sean O'Malley1, Stephen H Leppla2, Alan T Johnson3.
Abstract
Anthrax is a highly lethal disease caused by the Gram-(+) bacteria Bacillus anthracis. Edema toxin (ET) is a major contributor to the pathogenesis of disease in humans exposed to B. anthracis. ET is a bipartite toxin composed of two proteins secreted by the vegetative bacteria, edema factor (EF) and protective antigen (PA). Our work towards identifying a small molecule inhibitor of anthrax edema factor is the subject of this letter. First we demonstrate that the small molecule probe 5'-Fluorosulfonylbenzoyl 5'-adenosine (FSBA) reacts irreversibly with EF and blocks enzymatic activity. We then show that the adenosine portion of FSBA can be replaced to provide more drug-like molecules which are up to 1000-fold more potent against EF relative to FSBA, display low cross reactivity when tested against a panel of kinases, and are nanomolar inhibitors of EF in a cell-based assay of cAMP production.Entities:
Keywords: Anthrax; Covalent inhibitor; Edema factor
Mesh:
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Year: 2017 PMID: 29198864 PMCID: PMC5875723 DOI: 10.1016/j.bmcl.2017.11.040
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823