Structure-based design, synthesis, and evaluation of conformationally constrained mimetics of the second mitochondria-derived activator of caspase that target the X …
H Sun, Z Nikolovska-Coleska, CY Yang… - Journal of medicinal …, 2004 - ACS Publications
Journal of medicinal chemistry, 2004•ACS Publications
A successful structure-based design of conformationally constrained second mitochondria-
derived activator of caspase (Smac) mimetics that target the XIAP/caspase-9 interaction site
is described. The most potent Smac mimetic 12d has a K i of 350 nM for binding to the XIAP
BIR3 domain protein. 12d is found to be effective in enhancing apoptosis induced by
cisplatin in PC-3 human prostate cancer cells.
derived activator of caspase (Smac) mimetics that target the XIAP/caspase-9 interaction site
is described. The most potent Smac mimetic 12d has a K i of 350 nM for binding to the XIAP
BIR3 domain protein. 12d is found to be effective in enhancing apoptosis induced by
cisplatin in PC-3 human prostate cancer cells.
A successful structure-based design of conformationally constrained second mitochondria-derived activator of caspase (Smac) mimetics that target the XIAP/caspase-9 interaction site is described. The most potent Smac mimetic 12d has a Ki of 350 nM for binding to the XIAP BIR3 domain protein. 12d is found to be effective in enhancing apoptosis induced by cisplatin in PC-3 human prostate cancer cells.
ACS Publications