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|Title:||Structure-activity relationship studies of phenanthridine-based Bcl-X L inhibitors|
|Citation:||Bernardo, P.H., Wan, K.-F., Sivaraman, T., Xu, J., Moore, F.K., Hung, A.W., Mok, H.Y.K., Yu, V.C., Chai, C.L.L. (2008-11-13). Structure-activity relationship studies of phenanthridine-based Bcl-X L inhibitors. Journal of Medicinal Chemistry 51 (21) : 6699-6710. ScholarBank@NUS Repository. https://doi.org/10.1021/jm8005433|
|Abstract:||Despite their structural similarities, the natural products chelerythrine (5) and sanguinarine (6) target different binding sites on the pro-survival Bcl-XL protein. This paper details the synthesis of phenanthridine-based analogues of the natural products that were used to probe this difference in binding profiles. The inhibitory constants for these compounds were then measured in a fluorescence polarization assay against Bcl-XL and the tagged Bak-BH3 peptide. The results led to structure-activity relationship studies, which identified the structural motifs required for binding-site specificity as well as inhibitory activity. We also identified synthetic analogues of the natural products that display similar binding modes but with more potent IC50 values. © 2008 American Chemical Society.|
|Source Title:||Journal of Medicinal Chemistry|
|Appears in Collections:||Staff Publications|
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