Exploiting differences in caspase-2 and-3 S 2 subsites for selectivity: Structure-based design, solid-phase synthesis and in vitro activity of novel substrate-based …

…, F Krieger, M Meniconi, I Muñoz-Sanjuán…

文献索引：Maillard, Michel C.; Brookfield, Frederick A.; Courtney, Stephen M.; Eustache, Florence M.; Gemkow, Mark J.; Handel, Rebecca K.; Johnson, Laura C.; Johnson, Peter D.; Kerry, Mark A.; Krieger, Florian; Meniconi, Mirco; Munoz-Sanjuan, Ignacio; Palfrey, Jordan J.; Park, Hyunsun; Schaertl, Sabine; Taylor, Malcolm G.; Weddell, Derek; Dominguez, Celia Bioorganic and Medicinal Chemistry, 2011 , vol. 19, # 19 p. 5833 - 5851

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被引用次数: 15

摘要

Several caspases have been implicated in the pathogenesis of Huntington's disease (HD); however, existing caspase inhibitors lack the selectivity required to investigate the specific involvement of individual caspases in the neuronal cell death associated with HD. In order to explore the potential role played by caspase-2, the potent but non-selective canonical Ac- VDVAD-CHO caspase-2 inhibitor 1 was rationally modified at the P2 residue in an attempt ...