Abstract
Carbonic anhydrase inhibitors (CAI) are valuable molecules as they have several therapeutic applications, including anti-glaucoma activity. In this study, inhibition of three human carbonic anhydrase (hCA, EC 4.2.1.1) isozymes I, II and VI with a series of bisphenol and bromophenol derivatives was investigated. Molecular docking studies of a set of such inhibitors within CA I and II were also performed. K(I) values of the molecules 2-9 were in the range of 10.025-892.109 μM for hCA I, 1.437-59.107 μM for hCA II and 11.143-919.182 μM for hCA VI, respectively. Reported inhibitory activities of molecules 2-9 will assist in better understanding of structure-activity relationship studies of CAI.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carbonic Anhydrase I / antagonists & inhibitors*
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Carbonic Anhydrase I / metabolism
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Carbonic Anhydrase II / antagonists & inhibitors*
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Carbonic Anhydrase II / metabolism
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Carbonic Anhydrase IV / antagonists & inhibitors*
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Carbonic Anhydrase IV / metabolism
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Carbonic Anhydrase Inhibitors / chemical synthesis
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Carbonic Anhydrase Inhibitors / chemistry
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Carbonic Anhydrase Inhibitors / pharmacology*
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Dose-Response Relationship, Drug
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Humans
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Kinetics
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Models, Molecular
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Molecular Structure
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Phenols / chemical synthesis
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Phenols / chemistry
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Phenols / pharmacology*
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Structure-Activity Relationship
Substances
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Carbonic Anhydrase Inhibitors
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Phenols
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Carbonic Anhydrase I
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Carbonic Anhydrase II
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Carbonic Anhydrase IV
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CA4 protein, human