Oxethazaine is a bioactive molecule with a diverse profile of inhibitory activities. It effectively inhibits the binding of Batrachotoxinin [3H]BTX-B to high-affinity sites on voltage-dependent sodium channels, with an IC50 value of 2300.0 nM and an inhibition rate of 83.9% at a 10 µM concentration. The compound also targets several enzymes, including Cytochrome P450 2C19, 2D6, and 3A4, and proteins such as Sfp phosphopantetheinyl transferase, 15-hLO, and 15-hLO-2. It demonstrates activity against the importin beta complex dissociation, RanGTP-induced Rango, Polymerase Iota, T. brucei phosphofructokinase, and ATXN expression, and induces DNA re-replication in SW480 colon adenocarcinoma cells. Moreover, Oxethazaine inhibits human tyrosyl-DNA phosphodiesterase 1 both in the presence and absence of CPT and shows potential to block the entry of viruses like Marburg and Ebola Virus.
In addition, it functions as a BSEP inhibitor with an IC50 value of less than 10,000.0 nM in regulating ATP-dependent [3H]-taurocholate transport. For antiviral activity, Oxethazaine inhibits SARS-CoV-2 induced cytotoxicity in VERO-6 and Caco-2 cells, albeit with varying effectiveness, showing inhibition rates ranging from 0.21% to 24.59% at a 10 µM concentration. It also exhibits modest inhibition of the SARS-CoV-2 3CL-Pro protease and has IC50 values ranging from 18,600.0 nM to 18,620.87 nM in VERO-E6 cell assays with a CC50 value of 26,300.0 nM, indicating its toxicity limits.
In enzymatic studies, Oxethazaine shows inhibitory activity against human HDAC6, achieving 12.09% inhibition with a commercial peptide and 5.97% with a custom peptide. These diverse bioactivities make Oxethazaine a molecule of significant interest across various biological pathways and potential therapeutic applications..
Note: Summary generated by AI. Data source: ChEMBL 