A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors
Research into histone deacetylases (HDACs) has experienced a remarkable surge in recent years. These enzymes are key regulators of several fundamental biological processes, often associated with severe and potentially fatal diseases. Inhibition of their activity represents a promising therapeutic ap...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-11-01
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| Series: | Pharmaceuticals |
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| Online Access: | https://www.mdpi.com/1424-8247/16/12/1639 |
| _version_ | 1797379723007885312 |
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| author | Aliki Drakontaeidi Eleni Pontiki |
| author_facet | Aliki Drakontaeidi Eleni Pontiki |
| author_sort | Aliki Drakontaeidi |
| collection | DOAJ |
| description | Research into histone deacetylases (HDACs) has experienced a remarkable surge in recent years. These enzymes are key regulators of several fundamental biological processes, often associated with severe and potentially fatal diseases. Inhibition of their activity represents a promising therapeutic approach and a prospective strategy for the development of new therapeutic agents. A critical aspect of their inhibition is to achieve selectivity in terms of enzyme isoforms, which is essential to improve treatment efficacy while reducing undesirable pleiotropic effects. The development of computational chemistry tools, particularly molecular docking, is greatly enhancing the precision of designing molecules with inherent potential for specific activity. Therefore, it was considered necessary to review the molecular docking studies conducted on the major isozymes of the enzyme in order to identify the specific interactions associated with each selective HDAC inhibitor. In particular, the most critical isozymes of HDAC (1, 2, 3, 6, and 8) have been thoroughly investigated within the scope of this review. |
| first_indexed | 2024-03-08T20:27:06Z |
| format | Article |
| id | doaj.art-8a66533bb98e48809453a6a25dc64224 |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-08T20:27:06Z |
| publishDate | 2023-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pharmaceuticals |
| spelling | doaj.art-8a66533bb98e48809453a6a25dc642242023-12-22T14:31:16ZengMDPI AGPharmaceuticals1424-82472023-11-011612163910.3390/ph16121639A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective InhibitorsAliki Drakontaeidi0Eleni Pontiki1Department of Pharmaceutical Chemistry, School of Pharmacy, Faculty of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceDepartment of Pharmaceutical Chemistry, School of Pharmacy, Faculty of Health Sciences, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceResearch into histone deacetylases (HDACs) has experienced a remarkable surge in recent years. These enzymes are key regulators of several fundamental biological processes, often associated with severe and potentially fatal diseases. Inhibition of their activity represents a promising therapeutic approach and a prospective strategy for the development of new therapeutic agents. A critical aspect of their inhibition is to achieve selectivity in terms of enzyme isoforms, which is essential to improve treatment efficacy while reducing undesirable pleiotropic effects. The development of computational chemistry tools, particularly molecular docking, is greatly enhancing the precision of designing molecules with inherent potential for specific activity. Therefore, it was considered necessary to review the molecular docking studies conducted on the major isozymes of the enzyme in order to identify the specific interactions associated with each selective HDAC inhibitor. In particular, the most critical isozymes of HDAC (1, 2, 3, 6, and 8) have been thoroughly investigated within the scope of this review.https://www.mdpi.com/1424-8247/16/12/1639histone deacetylasesmolecular dockingisoformsinteractionsenzyme inhibition |
| spellingShingle | Aliki Drakontaeidi Eleni Pontiki A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors Pharmaceuticals histone deacetylases molecular docking isoforms interactions enzyme inhibition |
| title | A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors |
| title_full | A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors |
| title_fullStr | A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors |
| title_full_unstemmed | A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors |
| title_short | A Review on Molecular Docking on HDAC Isoforms: Novel Tool for Designing Selective Inhibitors |
| title_sort | review on molecular docking on hdac isoforms novel tool for designing selective inhibitors |
| topic | histone deacetylases molecular docking isoforms interactions enzyme inhibition |
| url | https://www.mdpi.com/1424-8247/16/12/1639 |
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