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Synthesis and Biological Activity of Novel Thiourea Derivatives as Carbonic Anhydrase Inhibitors

Synthesis and Biological Activity of Novel Thiourea Derivatives as Carbonic Anhydrase Inhibitors

Neslihan Korkmaz, Oday A Obaidi, Murat Senturk, Demet Astley, Deniz Ekinci, Claudiu T Supuran

J Enzyme Inhib Med Chem. 2015 Feb;30(1):75-80.

PMID: 24666304

Abstract:

A new series of chiral thiourea derivatives (5a-5c) and thiourea containing benzimidazole moieties (9b-9e) were synthesized from different amino acids (l-valine, l-isoleucine, l-methionine, l-phenylalanine, and d-phenylglycine). The compounds were characterized and tested against the two most studied members of the pH regulatory enzyme family, carbonic anhydrase (CA, EC 4.2.1.1). KI values of the novel compounds were measured in the range of 3.4-73.6 μM for hCA I isozyme and 8.7-1.44.2 μM for hCA II isozyme, respectively. Phenol was also tested as standard in order to understand the structure activity relationship and the clinically used sulfonamide acetazolamide was tested for comparison reasons. All of the compounds exhibited competitive inhibition with 4-nitrophenylacetate as substrate.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP14949009	Acetazolamide Related Compound D		14949-00-9	Price

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