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Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and II.
J Enzyme Inhib Med Chem. 2016; 31(1):31-7.JE

Abstract

A 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.

Authors+Show Affiliations

a Department of Chemistry , Istanbul Technical University , Istanbul , Turkey .b School of Medicine, Bahcesehir University , Istanbul , Turkey .c Department of Biophysics , School of Medicine, Bahcesehir University , Istanbul , Turkey .d Department of Chemistry, Art and Science Faculty , Agri Ibrahim Cecen University , Agri , Turkey , and.e School of Health, Gumushane University , Gumushane , Turkey.e School of Health, Gumushane University , Gumushane , Turkey.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

25676327

Citation

Ekhteiari Salmas, Ramin, et al. "Kinetic and in Silico Studies of Hydroxy-based Inhibitors of Carbonic Anhydrase Isoforms I and II." Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 31, no. 1, 2016, pp. 31-7.
Ekhteiari Salmas R, Mestanoglu M, Durdagi S, et al. Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and II. J Enzyme Inhib Med Chem. 2016;31(1):31-7.
Ekhteiari Salmas, R., Mestanoglu, M., Durdagi, S., Sentürk, M., Kaya, A. A., & Kaya, E. Ç. (2016). Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and II. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(1), 31-7. https://doi.org/10.3109/14756366.2014.1003216
Ekhteiari Salmas R, et al. Kinetic and in Silico Studies of Hydroxy-based Inhibitors of Carbonic Anhydrase Isoforms I and II. J Enzyme Inhib Med Chem. 2016;31(1):31-7. PubMed PMID: 25676327.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Kinetic and in silico studies of hydroxy-based inhibitors of carbonic anhydrase isoforms I and II. AU - Ekhteiari Salmas,Ramin, AU - Mestanoglu,Mert, AU - Durdagi,Serdar, AU - Sentürk,Murat, AU - Kaya,A Afşin, AU - Kaya,Elif Çelenk, Y1 - 2015/02/13/ PY - 2015/2/14/entrez PY - 2015/2/14/pubmed PY - 2016/10/8/medline KW - ADME KW - CA inhibitors KW - carbonic anhydrase KW - molecular docking simulations SP - 31 EP - 7 JF - Journal of enzyme inhibition and medicinal chemistry JO - J Enzyme Inhib Med Chem VL - 31 IS - 1 N2 - A 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. SN - 1475-6374 UR - https://www.unboundmedicine.com/medline/citation/25676327/Kinetic_and_in_silico_studies_of_hydroxy_based_inhibitors_of_carbonic_anhydrase_isoforms_I_and_II_ L2 - http://www.tandfonline.com/doi/full/10.3109/14756366.2014.1003216 DB - PRIME DP - Unbound Medicine ER -