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Phospholipases are one of the principal toxic enzymes in snake venoms inducing a wide variety of pharmacological effects after envenomation. Natural inhibitors from plants are known to inhibit the toxic enzyme activities of snake venoms. In this study, ethanol crude extract of  M. oleifera  leaves was partitioned using n-hexane and ethyl acetate after which fractionation was done using column and thin layer chromatography. Subsequently, the inhibitory activities of the crude extract and sub-fractions of  M. oleifera  were investigated against phospholipases A 2  isolated from  Naja haje  and  Naja nigricollis  venoms using  in vitro  and  in-silico  approaches while EchiTab-PLUS polyvalent antivenom was used as the standard drug. The molecular weight of isolated  N. haje  phospholipase A 2  (NH-PL) and  N. nigricollis  phospholipase A 2  (NN-PL) were 24.11 and 35.22 kDa respectively. NH-PL enzyme had a specific activity of 2.70 μM/min/mg substrate while NN-PL activity was 2.10 μM/min/mg substrate. The K m  of NH-PL was 0.330 μM with V max  of 0.085 μM/mL min while NN-PL had V max  of 0.198 μM/mL.min and K m  of 0.670 μM.  M. oleifera  n-hexane sub-fraction 5 (MOLH5) exhibited a total inhibition of NN-PL and NH-PL enzyme activities at all concentrations used. Molecular docking of the phytoconstituents of MOLH5 against the catalytic site of phospholipase A 2  revealed 2-Hydrazino-8-hydroxy-4-phenylquinoline as the lead compound and a potential drug candidate with a docking score of −6.789 kcal/mol. Findings indicated that MOLH5 possesses phospholipase A 2  natural inhibitors that could be explored as a therapy for snake envenoming.

toxin reviews

Inhibition of phospholipase A 2  from  Naja haje  and  Naja nigricollis  venoms by active fraction of  Moringa oleifera  leaves:  in vitro  and  in silico  methods