Background: The catalytically active site of CA enzyme is Zn (II) bound hydroxide ion part
which acts as a strong nucleophile (at neutral pH) on the CO2 molecule bound in a hydrophobic pocket
nearby. We designed a series of thiazolidinone molecules which are able to approach the active side by
way of hydrophobic part and may interact with the hydroxide and Zn (II) by ring opening of thiazolidinone.
Methods: Thirteen novel aminoindane thiazolidinone derivatives, 2a-m were synthesized, characterized
and their inhibitory effects on the activity of purified human carbonic anhydrase (hCA) I and II were
evaluated. hCA I and II from human erythrocytes were purified by a simple one step procedure by using
Sepharose 4B-L-tyrosine-sulphanilamide affinity column.
Results: In vitro results showed that all compounds were inhibited by the CA izoenzymes activity. 2d
was found to be most active compound IC50=6.75 μM and 7.55 μM for hCA I and hCA II, respectively.
Conclusion: New aminoindane thiazolidinone derivatives have been designed, synthesized and evaluated
as Carbonic Anhydrase Inhibitors. According to the results, these compounds can be conceivable as
new candidates for the treatment of the illness that CAI and CAII enzyme inhibitors are used in the