Structural, enzymatic and pharmacological profiles of AplTX-II - A basic sPLA2 (D49) isolated from the Agkistrodon piscivorus leucostoma snake venom

A basic sPLA 2 (D49) from the venom of snake Agkistrodon piscivorus leucostoma (AplTX-II) was isolated, purified and characterized. We determined enzymatic pharmacological profiles this toxin. AplTX-II isolated with a high level purity through reverse phase chromatography molecular exclusion. The enzyme showed pI 9.48 weight 14,003 Da. activity depended on Ca 2+ pH temperature. comparison primary structure other s revealed that presented all structural reasons expected for s. Additionally, we have resolved its docked synthetic substrate NOBA (4-nitro-3-octanoyloxy benzoic acid) by homology modeling, performed MD simulations explicit solvent. Structural similarities were found between enzyme's modeled X-Ray structures, available in PDB database. active-site water molecules spontaneously adopted stable positions established interactions full agreement reaction mechanism, proposed physiological substrate, suggesting hydrolysis is an excellent model to study phospholipid hydrolysis.