Kinetic and toxicological effects of synthesized palladium(II) complex on snake venom ) acetylcholinesterase.

BACKGROUND

The venom of the krait (), an Elapidae snake, is highly toxic to humans and contains a great amount of acetylcholinesterase (AChE). The enzyme AChE provokes the hydrolysis of substrate acetylcholine (ACh) in the nervous system and terminates nerve impulse. Different inhibitors inactivate AChE and lead to ACh accumulation and disrupted neurotransmission.

METHODS

The present study was designed to evaluate the effect of palladium(II) complex as antivenom against krait venom AChE using kinetics methods.

RESULTS

Statistical analysis showed that krait venom AChE inhibition decreases with the increase of Pd(II) complex (0.025-0.05 µM) and exerted 61% inhibition against the AChE at a fixed concentration (0.5 mM) of ACh. Kinetic analysis using the Lineweaver Burk plot showed that Pd(II) caused a competitive inhibition. The compound Pd(II) complex binds at the active site of the enzyme. It was observed that (Michaelis-Menten constant of AChE-ACh into AChE and product) increased from 0.108 to 0.310 mM (45.74 to 318.35%) and remained constant with an increase of Pd(II) complex concentrations. In AChE was found to increase from 0.0912 to 0.025 µM (29.82-72.58%) and did not affect the with an increase of ACh from (0.05-1 mM). (inhibitory constant) was estimated to be 0.029µM for snake venom; while the was estimated to be 0.4 mM. The calculated IC for Pd(II) complex was found to be 0.043 µM at constant ACh concentration (0.5 mM).

CONCLUSIONS

The results show that the Pd(II) complex can be deliberated as an inhibitor of AChE.