The effects of some bromophenols on human carbonic anhydrase isoenzymes

These results showed that all bromophenol derivatives had higher affinity toward hCA II than that of hCA I isoform

Parham Taslimi; İlhami Gülçin; Necla Öztaşkın; Yasin Çetinkaya; Süleyman Göksu; Saleh H. Alwasel; Claudiu T. Supuran

2015

Scholarcy highlights

  • Carbonic anhydrases are biological catalysts for the interconversion of carbon dioxide and water to bicarbonate: CAs are polifunctional enzymes which play a crucial role in different physiological and biochemical processes such as acid–base homeostasis, respiratory gas exchange, ionic transport, electrolytes secretion, muscular contraction in vertebrates, photosynthesis in cyanobacteria, plants and algae, synthesis of fatty acids, biosynthetic reactions including ureagenesis and gluconeogenesis
  • It was reported that the bromophenol derivatives coordinate to the active site Zn2+ and to block the reaction catalysis
  • It was found that hCA I, II and VI were inhibited by a series of bisphenol and bromophenol derivatives
  • It was demonstrated that dimethoxy-bromophenol derivatives incorporating cyclopropane moieties have shown picomolar inhibition against cytosolic CA I, II and tumor-associated CA IX, and XII9
  • It is well known that bromophenol derivatives had some biological activities including anti-oxidant and radical scavenging, acetylcholine esterase inhibition properties
  • All bromophenol derivatives have shown similar hCA II inhibition properties. These results showed that all bromophenol derivatives had higher affinity toward hCA II than that of hCA I isoform

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