Vol. 7, Issue 1, Part G (2025)

Carbonic anhydrase II (CA II), a zinc-containing metalloenzyme, plays a vital role in maintaining acid-base balance, respiration, and various physiological processes. Given its involvement in pathological conditions such as glaucoma, epilepsy, cancer, and osteoporosis, CA II has emerged as a key target for therapeutic intervention. This review comprehensively examines the structural diversity of CA II inhibitors, encompassing sulfonamides, coumarins, phenols, and newer scaffolds, highlighting their interaction modes and structure-activity relationships. Mechanistic insights into inhibition pathways, including classical zinc-binding inhibition and non-classical mechanisms, are discussed to elucidate how chemical structure influences potency and selectivity. Furthermore, the review explores the role of molecular docking and computational modeling in understanding inhibitor binding, predicting affinity, and guiding rational drug design. Recent advances in docking methodologies and their integration with experimental data are emphasized to provide a holistic perspective. By synthesizing current knowledge from structural biology, enzymology, and in silico approaches, this review aims to support future efforts in the design of selective and potent CA II inhibitors with improved therapeutic potential.