Zinab Khadim Raheem, Muna Hasson Saoudi, Kasim Mohmmed Hello
Chemistry Department, College of Science, Al-Muthanna University, Al-Muthanna governorate,
Samawa, Iraq

Abstract
Carbonic anhydrase (CA) is an important biological target in cancer therapy, due to its vital role in
regulating intracellular pH and providing an acidic environment that promotes the growth and spread of
cancer cells. Tumor cells rely on aerobic glycolysis, which leads to the accumulation of acidic products
such as CO₂ and lactic acid, thus lowering the pH in tumor tissue. In this study, molecular docking
demonstrated that SA and OSA possess a high binding capacity to the active site of CA II, with SA
recording the highest binding energy (-8.13 kcal/mol). Hydrogen bonding was documented within the
active pocket, supporting the stability of the enzyme complex. CA was purified from red blood cells
using systematic steps that included hypotonic lysis, hemoglobin removal using chloroform and ethanol,
and precipitation with ammonium sulfate.
Subsequently, the effectiveness of nanocatalysts (Si@SA and Si@OSA-Dir) at different concentrations
(up to 500 µg/mL) was evaluated, demonstrating their ability to raise the pH of the medium and reduce
acidity. The Si@OSA-Dir catalyst demonstrated significant effectiveness in stabilizing pH at 8 within
20 minutes, while the other compounds reached pH 7.7, demonstrating their effectiveness in adjusting
acidity.The results indicate that these prepared compounds hold promise as CA inhibitors and have
potential applications in cancer treatment strategies by targeting the acid balance in the tumor
microenvironment.

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