In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets
A great number of sesquiterpenes are reported in the available literature as good antileishmanial leads. However, their mode of action at the molecular level has not been elucidated. The lack of molecular studies could be considered an impediment for studies seeking to improve sesquiterpene-based dr...
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-04-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/19/5/5550 |
| _version_ | 1819266590895505408 |
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| author | Freddy A. Bernal Ericsson Coy-Barrera |
| author_facet | Freddy A. Bernal Ericsson Coy-Barrera |
| author_sort | Freddy A. Bernal |
| collection | DOAJ |
| description | A great number of sesquiterpenes are reported in the available literature as good antileishmanial leads. However, their mode of action at the molecular level has not been elucidated. The lack of molecular studies could be considered an impediment for studies seeking to improve sesquiterpene-based drug design. The present in silico study allows us to make important observations about the molecular details of the binding modes of a set of antileishmanial sesquiterpenes against four drug-enzyme targets [pteridine reductase-1 (PTR1), N-myristoyl transferase (NMT), cysteine synthase (CS), trypanothione synthetase (TryS)]. Through molecular docking it was found that two sesquiterpene coumarins are promising leads for the PTR1 and TryS inhibition purposes, and some xanthanolides also exhibited better affinity towards PTR1 and CS binding. In addition, the affinity values were clustered by Principal Component Analysis and drug-like properties were analyzed for the strongest-docking sesquiterpenes. The results are an excellent starting point for future studies of structural optimization of this kind of compounds. |
| first_indexed | 2024-12-23T21:03:42Z |
| format | Article |
| id | doaj.art-2f9591929a734bbab88858d8a0ad4655 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-23T21:03:42Z |
| publishDate | 2014-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-2f9591929a734bbab88858d8a0ad46552022-12-21T17:31:17ZengMDPI AGMolecules1420-30492014-04-011955550556910.3390/molecules19055550molecules19055550In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based TargetsFreddy A. Bernal0Ericsson Coy-Barrera1Laboratorio de Química Bioorgánica, Departamento de Química, Facultad de Ciencias Básicas y Aplicadas, Universidad Militar Nueva Granada, Cundinamarca 250240, AA 49300, ColombiaLaboratorio de Química Bioorgánica, Departamento de Química, Facultad de Ciencias Básicas y Aplicadas, Universidad Militar Nueva Granada, Cundinamarca 250240, AA 49300, ColombiaA great number of sesquiterpenes are reported in the available literature as good antileishmanial leads. However, their mode of action at the molecular level has not been elucidated. The lack of molecular studies could be considered an impediment for studies seeking to improve sesquiterpene-based drug design. The present in silico study allows us to make important observations about the molecular details of the binding modes of a set of antileishmanial sesquiterpenes against four drug-enzyme targets [pteridine reductase-1 (PTR1), N-myristoyl transferase (NMT), cysteine synthase (CS), trypanothione synthetase (TryS)]. Through molecular docking it was found that two sesquiterpene coumarins are promising leads for the PTR1 and TryS inhibition purposes, and some xanthanolides also exhibited better affinity towards PTR1 and CS binding. In addition, the affinity values were clustered by Principal Component Analysis and drug-like properties were analyzed for the strongest-docking sesquiterpenes. The results are an excellent starting point for future studies of structural optimization of this kind of compounds.http://www.mdpi.com/1420-3049/19/5/5550Leishmaniain-Silicomolecular dockingsesquiterpene |
| spellingShingle | Freddy A. Bernal Ericsson Coy-Barrera In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets Molecules Leishmania in-Silico molecular docking sesquiterpene |
| title | In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets |
| title_full | In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets |
| title_fullStr | In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets |
| title_full_unstemmed | In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets |
| title_short | In-Silico Analyses of Sesquiterpene-Related Compounds on Selected Leishmania Enzyme-Based Targets |
| title_sort | in silico analyses of sesquiterpene related compounds on selected leishmania enzyme based targets |
| topic | Leishmania in-Silico molecular docking sesquiterpene |
| url | http://www.mdpi.com/1420-3049/19/5/5550 |
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