Synthesis of carbazole bearing pyridopyrimidine‐substituted sulfonamide derivatives and studies their carbonic anhydrase enzyme activity

Abstract

The synthesis of carbazole containing pyridopyrimidine-substituted sulfonamide derivatives (3a-i) and their inhibitory effects on human carbonic anhydrase (hCA) I and II were studied. Spectral data and elemental analysis confirmed the structures of the compounds synthesized. The results show that all the synthesized compounds inhibited the CA I and II activities. Among them, 3a was found to be the most active (K i : 14 µM) for hCA I and 3f (K i : 126 µM) for hCA II. K E Y W O R D S carbazole, carbonic anhydrase, pyridopyrimidine, sulfonamide

Preparation and characterization of doped hollow carbon spherical nanostructures with nickel and cobalt metals and their catalysis for the green synthesis of pyridopyrimidines

“…In eqn (1), k is the number of factors, and C 0 is the replicate number of the central point. According to eqn (1), three factors and ve central points are considered, so there was a total of 17 runs.…”

“…Pyridopyrimidines and relevant fused heterocycles are of importance as potential bioactive molecules. They have been extensively applied in medicinal, 1,2 and biological chemistry [3][4][5] due to the range of their available products that includes vast chemical variety and their ve feasible substitution localities. 6 Hollow nanostructures are a group of specic nanomaterials identied based on their morphologies.…”

Evaluation of carbonic anhydrase and paraoxonase inhibition activities and molecular docking studies of highly water-soluble sulfonated phthalocyanines

“…Acetazolamide (AAZ) is one of the best-known CAIs and also used as a standard in CA assays [27]. Whereas complexes and 2 showed much weaker inhibitory activity against hCA I and hCA II than AAZ (Ki of 250 nM and 12.1 nM against hCA I and hCA II, respectively) [28,29],they exhibited higher hCA I and II inhibitory activity than some synthesized compounds (Ki or IC50 values ranging between 75 µM and 620 µM against hCA I, between 126 µM and 427 µM against hCA II) reported as CAIs in the literature [30][31][32][33]. The sulphonamides (known as strong CAIs) bind in the deprotonated form to the catalytically critical Zn(II) ion in the enzyme active site [34,35], also contributing in extensive hydrogen bond and van der Waals interactions with amino acid residues of the enzyme active site, as reported in X-ray crystallographic studies of enzyme-inhibitor complexes [36].…”

An overview on synthetic and pharmaceutical prospective of pyrido[2,3‐d]pyrimidines scaffold

“…Compounds 58a and 58f had found to be the most active for inhibition of hCA I and hCA II. Carbonic anhydrase activity was evaluated by using esterase activity assay (Rifati-Nixha et al, 2019). Lavanya, Asharani and Thirumalai demonstrated the fused pyrido[2,3-d]pyrimidines (59a-c) and assessed for their anti-inflammatory activity.…”