Analogs of the RSK inhibitor SL0101: optimization of in vitro biological stability.
Analogs of the RSK inhibitor SL0101: optimization of in vitro biological stability.
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DOI：
10.1016/j.bmcl.2012.03.033
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发表时间：
2012-05-01
影响因子：
2.7
通讯作者：
Lannigan, Deborah A.
中科院分区：
文献类型：
--
作者：
Hilinski, Michael K.;Mrozowski, Roman M.;Clark, David E.;Lannigan, Deborah A.
The Ser/Thr protein kinase, RSK, is important in the etiology of tumor progression including invasion and motility. The natural product kaempferol-3-O-(3″,4″-di-O-acetyl-α-L-rhamnopyranoside), called SL0101, is a highly specific RSK inhibitor. Acylation of the rhamnose moiety is necessary for high affinity binding and selectivity. However, the acetyl groups can be cleaved by esterases, which accounts for the poor in vitro biological stability of SL0101. To address this problem a series of analogues containing acetyl group replacements were synthesized and their in vitro stability evaluated. Monosubstituted carbamate analogues of SL0101 showed improved in vitro biological stability while maintaining specificity for RSK. These results should facilitate the development of RSK inibitors derived from SL0101 as anticancer agents.
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影响因子：
16
作者：
Eisinger-Mathason, T. S. Karin;Andrade, Josefa;Groehler, Angela L.;Clark, David E.;Muratore-Schroeder, Tara L.;Pasic, Lejla;Smith, Jeffrey A.;Shabanowitz, Jeffrey;Hunt, Donald F.;Macara, Ian G.;Lannigan, Deborah A.
通讯作者：
Lannigan, Deborah A.
影响因子：
10.5
作者：
Smolen, Gromoslaw A.;Zhang, Jianmin;Haber, Daniel A.
通讯作者：
Haber, Daniel A.
影响因子：
2.7
作者：
Eisinger-Mathason, T. S. Karin;Andrade, Josefa;Lannigan, Deborah A.
通讯作者：
Lannigan, Deborah A.
影响因子：
3.5
作者：
Smith, Jeffrey A.;Maloney, David J.;Lannigan, Deborah A.
通讯作者：
Lannigan, Deborah A.
影响因子：
5.2
作者：
Shan, Mingde;O'Doherty, George A.
通讯作者：
O'Doherty, George A.