Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme
Inhibition of the β-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6....
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Taylor & Francis Group
2019-01-01
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| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
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| Online Access: | http://dx.doi.org/10.1080/14756366.2018.1564045 |
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doaj-75ae73187cad47438a2d344cb33f02892020-11-25T00:51:54ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742019-01-0134152853110.1080/14756366.2018.15640451564045Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzymeAtilla Akdemir0Andrea Angeli1Füsun Göktaş2Pınar Eraslan Elma3Nilgün Karalı4Claudiu T. Supuran5Bezmialem Vakif UniversityUniversita degli Studi di FirenzeIstanbul UniversityIstanbul UniversityIstanbul UniversityUniversita degli Studi di FirenzeInhibition of the β-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4-63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies.http://dx.doi.org/10.1080/14756366.2018.1564045sulfonamidescandida glabratacarbonic anhydrasedocking |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Atilla Akdemir Andrea Angeli Füsun Göktaş Pınar Eraslan Elma Nilgün Karalı Claudiu T. Supuran |
| spellingShingle |
Atilla Akdemir Andrea Angeli Füsun Göktaş Pınar Eraslan Elma Nilgün Karalı Claudiu T. Supuran Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme Journal of Enzyme Inhibition and Medicinal Chemistry sulfonamides candida glabrata carbonic anhydrase docking |
| author_facet |
Atilla Akdemir Andrea Angeli Füsun Göktaş Pınar Eraslan Elma Nilgün Karalı Claudiu T. Supuran |
| author_sort |
Atilla Akdemir |
| title |
Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| title_short |
Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| title_full |
Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| title_fullStr |
Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| title_full_unstemmed |
Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| title_sort |
novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme |
| publisher |
Taylor & Francis Group |
| series |
Journal of Enzyme Inhibition and Medicinal Chemistry |
| issn |
1475-6366 1475-6374 |
| publishDate |
2019-01-01 |
| description |
Inhibition of the β-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4-63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies. |
| topic |
sulfonamides candida glabrata carbonic anhydrase docking |
| url |
http://dx.doi.org/10.1080/14756366.2018.1564045 |
| work_keys_str_mv |
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