PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes
Cyclic nucleotide phosphodiesterases 4 (PDE4) are a family of enzymes which specifically promote the hydrolysis and degradation of cAMP. The inhibition of PDE4 enzymes has been widely investigated as a possible alternative strategy for the treatment of a variety of respiratory diseases, including ch...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/14/11518 |
| _version_ | 1797589067428265984 |
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| author | Jian Jin Francesca Mazzacuva Letizia Crocetti Maria Paola Giovannoni Agostino Cilibrizzi |
| author_facet | Jian Jin Francesca Mazzacuva Letizia Crocetti Maria Paola Giovannoni Agostino Cilibrizzi |
| author_sort | Jian Jin |
| collection | DOAJ |
| description | Cyclic nucleotide phosphodiesterases 4 (PDE4) are a family of enzymes which specifically promote the hydrolysis and degradation of cAMP. The inhibition of PDE4 enzymes has been widely investigated as a possible alternative strategy for the treatment of a variety of respiratory diseases, including chronic obstructive pulmonary disease and asthma, as well as psoriasis and other autoimmune disorders. In this context, the identification of new molecules as PDE4 inhibitors continues to be an active field of investigation within drug discovery. This review summarizes the medicinal chemistry journey in the design and development of effective PDE4 inhibitors, analyzed through chemical classes and taking into consideration structural aspects and binding properties, as well as inhibitory efficacy, PDE4 selectivity and the potential as therapeutic agents. |
| first_indexed | 2024-03-11T01:01:04Z |
| format | Article |
| id | doaj.art-caa0624b282847108245539e91284412 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T01:01:04Z |
| publishDate | 2023-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-caa0624b282847108245539e912844122023-11-18T19:40:43ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-07-0124141151810.3390/ijms241411518PDE4 Inhibitors: Profiling Hits through the Multitude of Structural ClassesJian Jin0Francesca Mazzacuva1Letizia Crocetti2Maria Paola Giovannoni3Agostino Cilibrizzi4Institute of Pharmaceutical Science, King’s College London, Stamford Street, London SE1 9NH, UKSchool of Health, Sport and Bioscience, University of East London, London E15 4LZ, UKNeurofarba Department, Pharmaceutical and Nutraceutical Section, Via Ugo Schiff 6, Sesto Fiorentino, University of Florence, 50019 Florence, ItalyNeurofarba Department, Pharmaceutical and Nutraceutical Section, Via Ugo Schiff 6, Sesto Fiorentino, University of Florence, 50019 Florence, ItalyInstitute of Pharmaceutical Science, King’s College London, Stamford Street, London SE1 9NH, UKCyclic nucleotide phosphodiesterases 4 (PDE4) are a family of enzymes which specifically promote the hydrolysis and degradation of cAMP. The inhibition of PDE4 enzymes has been widely investigated as a possible alternative strategy for the treatment of a variety of respiratory diseases, including chronic obstructive pulmonary disease and asthma, as well as psoriasis and other autoimmune disorders. In this context, the identification of new molecules as PDE4 inhibitors continues to be an active field of investigation within drug discovery. This review summarizes the medicinal chemistry journey in the design and development of effective PDE4 inhibitors, analyzed through chemical classes and taking into consideration structural aspects and binding properties, as well as inhibitory efficacy, PDE4 selectivity and the potential as therapeutic agents.https://www.mdpi.com/1422-0067/24/14/11518phosphodiesterases 4PDE4 inhibitorsstructural analysisPDE4 selectivityrespiratory diseasesdual activity |
| spellingShingle | Jian Jin Francesca Mazzacuva Letizia Crocetti Maria Paola Giovannoni Agostino Cilibrizzi PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes International Journal of Molecular Sciences phosphodiesterases 4 PDE4 inhibitors structural analysis PDE4 selectivity respiratory diseases dual activity |
| title | PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes |
| title_full | PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes |
| title_fullStr | PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes |
| title_full_unstemmed | PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes |
| title_short | PDE4 Inhibitors: Profiling Hits through the Multitude of Structural Classes |
| title_sort | pde4 inhibitors profiling hits through the multitude of structural classes |
| topic | phosphodiesterases 4 PDE4 inhibitors structural analysis PDE4 selectivity respiratory diseases dual activity |
| url | https://www.mdpi.com/1422-0067/24/14/11518 |
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