inhibitory effect of newly prepared pyrazole derivatives against alpha-amylase in pancreatic cancer cell

This study focuses on synthesizing three pyrazole derivatives, namely b, c, and d. fourier transform infrared spectroscopy (ftir) and proton nuclear magnetic resonance spectroscopy ( 1h-nmr) were used to study the synthesized derivatives. pyrazole derivative b was produced from the chalcone derivative (a) reaction with (4-nitrophenyl) hydrazine. the pyrazole derivatives c and d were produced from the reaction of chalcone derivative (a) with hydrazide derivatives (n-(2-oxopropyl)benzamide and 3-acetyl-1- cyclopropyl-6-fluoro-7-(piperazine-1-yl)quinolin-4(1h)-one), respectively. the purification of α-amylase was conducted on pancreatic cancer patients from iraq, employing three distinct purifying techniques. the experiment yielded a high level of enzyme activity, specifically 7 u/ml and a specific activity of 8.75 u/mg protein. these results were achieved using an ammonium sulfate saturation ratio of 65%. the graph shows a peak in enzyme activity at 3.75 u/ml in the elution area. this peak, fraction 55, has 11.3 u/mg protein activity. the stability of α-amylase was constant over a ph range of 5.0 to 9.0. in the ph range of 6 to 7, enzyme stability is highest at ph 7. at ph 5 and 9, strength decreased. the enzyme was less active at ph 5 and 6 but more active at ph 7 and 9. however, enzyme activity peaked at ph 8.0. the α-amylase enzyme maintained 100% activity at 27-37 °c, demonstrating stability. however, enzyme activity decreased to 50% at 47 °c when temperature increased. the inhibitory effect of bis-chalcone and pyrazole derivatives increased with concentration. the results show that compound b has the most significant inhibitory efficacy, at 50%.