Exploring Natural Product Derivatives having Carbonic Anhydrase Inhibitory Activity

Abstract

Carbonic anhydrase is an enzyme which plays an active role in many biological functions of the human body. It is omnipresent in all the biological organisms with eight different genetic families. Its primary role is to catalyze the reversible hydration of CO2 to bicarbonate and protons. Though it is beneficial in many aspects it is also equally important for the cancer cells because of its pH regulatory nature. For tumor cells to survive and metastasis the regulation of pH and creating a hypoxia condition is very much needed, as Carbonic anhydrase is an extended family of sixteen isozymes, some of them are very essential for tumor cells. Many research is going on to inhibit the selective enzyme which is over expressed in the tumor cells. To be exact Carbonic anhydrase IX and XII are the most important enzymes overexpressed in the tumor cells. Sulfonamides, along with their bioisosters sulfonamides and sulfamates, have been employed for decades in treating conditions like glaucoma, epilepsy, and diuretics. Notably, this class of compounds has been extensively studied for its role as carbonic anhydrase inhibitors, showcasing their significant use and exploration in various therapeutic applications. In recent years, there has been a notable shift in the study of Carbonic anhydrase inhibitors towards natural products in addition to synthetic derivatives. Traditional drug design methods have historically yielded synthetic CAIs, but the exploration of Natural products derivatives has significantly advanced the field. Natural products, such as psammaplin C and altemicidin, containing primary sulfonamide or sulfamate groups, are gaining attention. The chemical diversity, binding specificity, and interaction tendencies of natural product derivatives make them appealing for molecular probes in research.