Carbonic anhydrase inhibitors: Two-prong versus mono-prong inhibitors of isoforms I, II, IX, and XII exemplified by photochromic cis-1,2-α-dithienylethene derivatives
| Autor: | Claudiu T. Supuran, Daniel Vomasta, Burkhard König, Alessio Innocenti |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Gene isoform
Carbonic Anhydrase I Photochemistry Stereochemistry Carbonic anhydrase II Clinical Biochemistry Pharmaceutical Science Ether Carbonic Anhydrase II Biochemistry Isozyme Structure-Activity Relationship Photochromism chemistry.chemical_compound Antigens Neoplasm Carbonic anhydrase Drug Discovery Humans Structure–activity relationship Carbonic Anhydrase IX Carbonic Anhydrase Inhibitors Molecular Biology Carbonic Anhydrases biology Organic Chemistry Isoenzymes chemistry biology.protein Molecular Medicine |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 19:1283-1286 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/j.bmcl.2009.01.079 |
| Popis: | We investigated the inhibition of five physiologically relevant CA isoforms with photochromic cis-1,2-alpha-dithienylethene-based compounds incorporating either a benzenesulfonamide and Cu(II)-iminodiacetic acid (IDA)-, bis-benzenesulfonamide-, bis-Cu(II)-IDA-, and bis-ethyleneglycol-methyl ether moieties, in both their open- and closed-ring forms. For hCA I the best inhibitors were the mono-prong bis-sulfonamide and the bis-Cu-IDA complexes (K(I)s of 2-3 nM) in their open form. For hCA II, best inhibitors were the open and closed forms of the mono-prong bis-sulfonamide (K(I)s of 13-18 nM). hCA IX was moderately inhibited by these compounds (K(I)s of 9-376 nM) whereas hCA XII and XIV were less susceptible to inhibition (K(I)s of 1.12-16.7 microM). |
| Databáze: | OpenAIRE |
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