Sensitivity of serum acetylcholine esterase toward derivatives of oxadiazole

الملخص EN

This work addresses the kinetic analysis of the interaction of some oxadiazoles (L1, L2, L3 and L4) in ethanol with serum acetylcholinesterase.

It was found that ethanol have inhibitory effect (25.18 %) on AChE enzyme for this reason niglicable it as solvent and instead of it use dimethyl sulfoxide which had no effect.

The % inhibition of L1, L2, L3 and L4 at 10-7 M was 54.67, 71.51, 45.42and 74.27 respectively and it elevated with increasing the concentration till at 10-1 M it reached 53.62, 99.08, 56.22and 99.43 respectively.

The effect of both L2 and L4 was reversible in nature.

Michaelis-Menten constant and maximum velocity for the hydrolysis of acetyl thiocholine iodide by AChE were determined in control and treated systems.

Line weaver–Burk plot and their secondary replots indicated that the nature of inhibition in both compounds was noncompetitive inhibition.

The value of Ki was estimated also.

The mechanism of action of these types of compounds acting as inhibitors to the AChE is suggested.