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Title: Structure-activity relationship studies of phenanthridine-based Bcl-X L inhibitors
Authors: 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.
Issue Date: 13-Nov-2008
Source: 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.
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
ISSN: 00222623
DOI: 10.1021/jm8005433
Appears in Collections:Staff Publications

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