Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors
A similarity search on the structural analogs of an inhibitor of BACE-1 with IC50 2.8 μM, which contained a P1 benzothiazole group together with a triazine ring linked by a secondary amine group, was described in this Letter and some more potent inhibitors against BACE-1 were identified. The most po...
| Main Authors: | , , , |
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| Format: | Journal Article |
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Pergamon
2010
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| Online Access: | http://hdl.handle.net/20.500.11937/48140 |
| _version_ | 1848758028554207232 |
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| author | Xu, W. Chen, G. Zhu, W. Zuo, Zhili |
| author_facet | Xu, W. Chen, G. Zhu, W. Zuo, Zhili |
| author_sort | Xu, W. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | A similarity search on the structural analogs of an inhibitor of BACE-1 with IC50 2.8 μM, which contained a P1 benzothiazole group together with a triazine ring linked by a secondary amine group, was described in this Letter and some more potent inhibitors against BACE-1 were identified. The most potent compound 5 (IC50 = 0.12 μM) increases the inhibitory potency by 24 folds. Our results suggest that a pyrrolidinyl side group at the P3′ and P4′ of the inhibitors are favored for strong inhibition and a small aromatic group at the P4 position is also essential to the potency. |
| first_indexed | 2025-11-14T09:37:29Z |
| format | Journal Article |
| id | curtin-20.500.11937-48140 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:37:29Z |
| publishDate | 2010 |
| publisher | Pergamon |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-481402019-02-19T04:26:47Z Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors Xu, W. Chen, G. Zhu, W. Zuo, Zhili FRET Virtual screening Bioassay BACE-1 A similarity search on the structural analogs of an inhibitor of BACE-1 with IC50 2.8 μM, which contained a P1 benzothiazole group together with a triazine ring linked by a secondary amine group, was described in this Letter and some more potent inhibitors against BACE-1 were identified. The most potent compound 5 (IC50 = 0.12 μM) increases the inhibitory potency by 24 folds. Our results suggest that a pyrrolidinyl side group at the P3′ and P4′ of the inhibitors are favored for strong inhibition and a small aromatic group at the P4 position is also essential to the potency. 2010 Journal Article http://hdl.handle.net/20.500.11937/48140 10.1016/j.bmcl.2010.08.111 Pergamon fulltext |
| spellingShingle | FRET Virtual screening Bioassay BACE-1 Xu, W. Chen, G. Zhu, W. Zuo, Zhili Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title | Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title_full | Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title_fullStr | Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title_full_unstemmed | Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title_short | Molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic BACE-1 inhibitors |
| title_sort | molecular docking and structure-activity relationship studies on benzothiazole based non-peptidic bace-1 inhibitors |
| topic | FRET Virtual screening Bioassay BACE-1 |
| url | http://hdl.handle.net/20.500.11937/48140 |