Sana Piri - Bioinformatics Lab., Department of Biology, School of Sciences, Razi University, Kermanshah, Iran.
Hamid Mahdiuni - Bioinformatics Lab., Department of Biology, School of Sciences, Razi University, Kermanshah, Iran.
Reza Khodarahmi - Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran.

In the present investigation, we analyzed the interaction of resorcinol and resveratrol and their sulfonamide derivatives with human carbonic anhydrase II (hCA II) using fluorescence spectroscopy, molecular docking and molecular dynamics simulation techniques.. Fluorescence data obtaining at three temperatures indicated that resveratrol and its sulfonamide derivative quenched intrinsic fluorescence of the enzyme through a static mechanism but resorcinol and its sulfonamide derivative increase intrinsic fluorescence of the enzyme through a static mechanism. Thermodynamic analysis of the quenching data indicated that hydrogen bonding and van der Waals interactions play important roles in the ligand binding. Based on computational data obtained by molecular docking and molecular dynamics simulation studies, hydrogen bonds are the main intermolecular forces for the ligand-hCA II interactions. In comparison with resveratrol and resorcinol, their sulfonamide derivatives bind stronger to hCA II. According to an assay method basing on fluorometric measurements, the sulfonamide derivatives had a greater inhibitory effect than the original compounds.

Carbonic Anhydrase II, resveratrol, resorcinol and sulfonamide derivatives.