Bismuth Complexes Inhibit the SARS Coronavirus

Development of chemical inhibitors of the SARS coronavirus: Viral helicase as a potential target

“…For example, bananins, which are adamantane derivatives in which vitamin B6 (pyridoxal) is directly conjugated, strongly inhibited the activity of SCV helicase in vitro and replication of SCV in cultured cells [29]. Exposure of bismuth compounds, which are clinically used as medications for treatment of a variety of gastrointestinal disorders [75], also exerted strong inhibitory effects on the DNA unwinding activity as well as the ATPase activity of SCV helicase, resulting in a retarded growth of SCV-infected cells [76,77]. Further, Lee et al recently identified some aryl diketoacids (ADKs) as chemical inhibitors of SCV helicase.…”

Recent advances in bioinorganic chemistry of bismuth

“…Various new bismuth-containing complexes have been synthesized and showed promising in vitro activities against H. pylori [17,18]. Importantly, some bismuthcontaining complexes have been demonstrated to exhibit new in vitro activities including antifungal, antiviral or even anticancer activities [19][20][21][22][23][24].…”

“…The antiviral activity of bismuth complexes was explored over the severe acute respiratory syndrome coronavirus (SARS-CoV), an enveloped, single-stranded RNA positive-strand virus that killed hundreds of people worldwide when is broken out in 2003 [30]. A series of bismuth complexes including bismuth nitrilotriacetate Bi(NTA), bismuth tricysteine Bi(Cys) 3 , RBC, bismuth ethylenediaminetetraacetate (Bi(EDTA)) as well as bismuth complexes with various N,O-containing chelate ligands including bismuth porphyrin complexes were examined against the SARS-CoV helicase [21,22], which was postulated to be the potential target for anti-SARS therapy [30]. The majority of bismuth complexes tested exhibited activities against SARS-CoV helicase ATPase and duplex-unwinding activities with the highest activities found for RBC and bismuth porphyrin complexes at IC 50 values of less than 1 mM.…”

Atlas of coronavirus replicase structure

“…Many excellent and exhaustive studies have based this mechanism of catalysis and the structure of the catalytic site architecture to design several different classes of peptidomimetic inhibitors targeted against M pro of coronaviruses (including SARS) and other pathogenic viruses. Several M pro inhibitors have also been structurally characterized (Akaji et al, 2011;Bacha et al, 2008;Chu et al, 2006;Chuck et al, 2013;Grum-Tokars et al, 2008;Lee et al, 2007;Lee et al, 2009;Lee et al, 2005;Shan and Xu, 2005;Shao et al, 2007;Turlington et al, 2013;Verschueren et al, 2008;Wei et al, 2006;Yang et al, 2006;Yang et al, 2003;Yang et al, 2007;Zhang et al, 2010;Zhu et al, 2011).…”