Human carbonic anhydrase (hCA) isoenzymes are zinc ion‐containing, widespread metalloenzymes and they classically play a role in pH homeostasis maintenance. CA inhibitors suppress the CA activity and their usage has been clinically established as antiglaucoma agents, antiepileptics, diuretics, and in some other disorders. Alzheimer's disease (AD) is a slowly progressive neurodegenerative disorder and a fatal disease of the brain. An advanced method to cure AD includes the strategy to design acetylcholinesterase (AChE) inhibitors. A novel series of pyrrole‐3‐one derivatives containing sulfa drugs (5a–i) were determined to be highly potent inhibitors for AChE and hCA I and hCA II (inhibitory constant [Ki] values are in the range of 6.50 ± 1.02–37.46 ± 4.12 nM, 1.20 ± 0.19–44.21 ± 1.09 nM, and 8.93 ± 1.58–46.86 ± 8.41 nM for AChE, hCA I, and hCA II, respectively). The designed compounds often show a more effective inhibition than the chemicals used as the standard. Among these compounds, 5f was the most effective compound against hCA I, and compound 5e was the most effective compound against hCA II. It was determined that compound 5c was the most effective inhibitor for AChE.

Thiazoles have attracted much synthetic interest due to their wide variety of biological properties and are important members of heterocyclic compounds. In recent years, studies on the synthesis of thiazole compounds have been increasing because of the properties of this core. In particular, the hybrid structures in which the thiazole ring and the other nuclei are linked have gained popularity. Hybrid structures are formed by the combination of different groups of chemical reactivity and biological activity characteristics. In this review, we highlight recent developments related to hybrid structures containing a thiazole core, recently developed as anticancer, antibacterial, anti-inflammatory, analgesic, anti-tubercular, antialzheimer and antidiabetic compounds.

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Inhibition of the Hsp90 function is an essential therapeutic approach and several inhibitors were designed as anti-cancer agents. These inhibitors are ATPases and they aim to deregulate Hsp90 folding function. ATPase proteins are common in human metabolism but they form nonspecific targets. Hsp90 functions as dimer with coordinating chaperones. Heat Shock Organizing Protein (Hop) forms a bridge between Hsp90 and Hsp70-Hsp40 complex to form Hsp90-Hsp70 coordination. Perturbing conformational changes of these Hsp proteins, dimer formation, and protein-protein interactions inhibit Hsp90 substrate protein folding function. This approach does not target all ATPase proteins but targets Hsp90 function solely. For this purpose, we designed compounds to block Hsp90 function. Moreover, molecular docking studies as well as competition analysis of the compounds were performed with Hsp90. Novel thiazolyl coumarine compounds were determined as valuable C-terminal Hsp90 inhibitors and provide promising templates for the drug design. Anticancer activities of these novel compounds were tested by employing human colon (DLD-1) and liver cancer (HepG2) cell lines. Thiazolyl coumarine compounds are found to be significant and useful for the treatment of human colon and liver cancer as evidenced by in vitro and in silico results.

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