Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors
The isatin scaffold is the constitutive fragment of several natural and synthetic bioactive molecules. Albeit several benzene sulphonamide-based carbonic anhydrase inhibitors (CAIs) have been reported, only recently isatin benzene sulphonamides have been studied and proposed as CAIs. In this study w...
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2017-01-01
|
| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/14756366.2016.1235042 |
| _version_ | 1819107043613605888 |
|---|---|
| author | Claudia Melis Rita Meleddu Andrea Angeli Simona Distinto Giulia Bianco Clemente Capasso Filippo Cottiglia Rossella Angius Claudiu T. Supuran Elias Maccioni |
| author_facet | Claudia Melis Rita Meleddu Andrea Angeli Simona Distinto Giulia Bianco Clemente Capasso Filippo Cottiglia Rossella Angius Claudiu T. Supuran Elias Maccioni |
| author_sort | Claudia Melis |
| collection | DOAJ |
| description | The isatin scaffold is the constitutive fragment of several natural and synthetic bioactive molecules. Albeit several benzene sulphonamide-based carbonic anhydrase inhibitors (CAIs) have been reported, only recently isatin benzene sulphonamides have been studied and proposed as CAIs. In this study we have designed, synthesised, and evaluated the biological activity of a series of differently substituted isatin-based benzene sulphonamides which have been designed for the inhibition of carbonic anhydrase isoforms. The activity of all the synthesised compounds was evaluated towards human carbonic anhydrase I, II, IX, and XII isozymes. Our results indicate that the nature and position of substituents on the isatin ring can modulate both activity and isozyme selectivity. |
| first_indexed | 2024-12-22T02:47:46Z |
| format | Article |
| id | doaj.art-8e3c55a9ca1043289f5af1d682be8f71 |
| institution | Directory Open Access Journal |
| issn | 1475-6366 1475-6374 |
| language | English |
| last_indexed | 2024-12-22T02:47:46Z |
| publishDate | 2017-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Enzyme Inhibition and Medicinal Chemistry |
| spelling | doaj.art-8e3c55a9ca1043289f5af1d682be8f712022-12-21T18:41:28ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742017-01-01321687310.1080/14756366.2016.12350421235042Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitorsClaudia Melis0Rita Meleddu1Andrea Angeli2Simona Distinto3Giulia Bianco4Clemente Capasso5Filippo Cottiglia6Rossella Angius7Claudiu T. Supuran8Elias Maccioni9University of CagliariUniversity of CagliariUniversità degli Studi di FirenzeUniversity of CagliariUniversity of CagliariIstituto di Bioscienze e Biorisorse, CNRUniversity of CagliariLaboratorio NMR e Tecnologie Bioanalitiche, Sardegna RicercheUniversità degli Studi di FirenzeUniversity of CagliariThe isatin scaffold is the constitutive fragment of several natural and synthetic bioactive molecules. Albeit several benzene sulphonamide-based carbonic anhydrase inhibitors (CAIs) have been reported, only recently isatin benzene sulphonamides have been studied and proposed as CAIs. In this study we have designed, synthesised, and evaluated the biological activity of a series of differently substituted isatin-based benzene sulphonamides which have been designed for the inhibition of carbonic anhydrase isoforms. The activity of all the synthesised compounds was evaluated towards human carbonic anhydrase I, II, IX, and XII isozymes. Our results indicate that the nature and position of substituents on the isatin ring can modulate both activity and isozyme selectivity.http://dx.doi.org/10.1080/14756366.2016.1235042Antitumour agentscarbonic anhydrase inhibitorsisatin hybrid molecules |
| spellingShingle | Claudia Melis Rita Meleddu Andrea Angeli Simona Distinto Giulia Bianco Clemente Capasso Filippo Cottiglia Rossella Angius Claudiu T. Supuran Elias Maccioni Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors Journal of Enzyme Inhibition and Medicinal Chemistry Antitumour agents carbonic anhydrase inhibitors isatin hybrid molecules |
| title | Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors |
| title_full | Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors |
| title_fullStr | Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors |
| title_full_unstemmed | Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors |
| title_short | Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors |
| title_sort | isatin a privileged scaffold for the design of carbonic anhydrase inhibitors |
| topic | Antitumour agents carbonic anhydrase inhibitors isatin hybrid molecules |
| url | http://dx.doi.org/10.1080/14756366.2016.1235042 |
| work_keys_str_mv | AT claudiamelis isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT ritameleddu isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT andreaangeli isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT simonadistinto isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT giuliabianco isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT clementecapasso isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT filippocottiglia isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT rossellaangius isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT claudiutsupuran isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors AT eliasmaccioni isatinaprivilegedscaffoldforthedesignofcarbonicanhydraseinhibitors |