2026-10-23T17:52:55Zhttps://gumushane-rdlopen.rawdatalibrary.net/oai/request

oai:gumushane-rdlopen.rawdatalibrary.net:gumushane/152612026-10-22T11:37:50Zopenairedrivercom_gumushane_10000col_gumushane_10001com_gumushane_10007col_gumushane_10180

Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and IIEkhteiari Salmas, RaminMestanoglu, MertDurdagi, SerdarSentürk, MuratKaya, A. AfşinKaya, Elif ÇelenkADMECA inhibitorscarbonic anhydrasemolecular docking simulationsA series of hydroxy and phenolic compounds have been assayed for the inhibition of two physiologically relevant carbonic anhydrase (CA, EC 4.2.1.1) isozymes, the cytosolic human isozymes I and II. The investigated molecules showed inhibition constants in the range of 1.07-4003 and 0.09-31.5 μM at the hCA I and hCA II enzymes, respectively. In order to investigate the binding mechanisms of these inhibitors, in silico studies were also applied. Molecular docking scores of the studied compounds are compared using three different scoring algorithms, namely Glide/SP, Glide/XP and Glide/IFD. In addition, different ADME (absorption, distribution, metabolism and excretion) analysis was performed. All the examined compounds were found within the acceptable range of pharmacokinetic profiles.Taylor and Francis Ltd2016Articlehttps://rdlopen.rawdatalibrary.net/r/gumushane/15261https://doi.org/10.3109/14756366.2014.10032161475-6366enJournal of Enzyme Inhibition and Medicinal Chemistryinfo:eu-repo/semantics/openAccessinfo:eu-repo/semantics/articlehttps://gumushane-rdlopen.rawdatalibrary.net/tr/items/gumushane/15261