Mechanistic and Structural Understanding of Uncompetitive Inhibitors of Caspase-6

نویسندگان

  • Christopher E. Heise
  • Jeremy Murray
  • Katherine E. Augustyn
  • Brandon Bravo
  • Preeti Chugha
  • Frederick Cohen
  • Anthony M. Giannetti
  • Paul Gibbons
  • Rami N. Hannoush
  • Brian R. Hearn
  • Priyadarshini Jaishankar
  • Cuong Q. Ly
  • Kinjalkumar Shah
  • Karen Stanger
  • Micah Steffek
  • Yinyan Tang
  • Xianrui Zhao
  • Joseph W. Lewcock
  • Adam R. Renslo
  • John Flygare
  • Michelle R. Arkin
چکیده

Inhibition of caspase-6 is a potential therapeutic strategy for some neurodegenerative diseases, but it has been difficult to develop selective inhibitors against caspases. We report the discovery and characterization of a potent inhibitor of caspase-6 that acts by an uncompetitive binding mode that is an unprecedented mechanism of inhibition against this target class. Biochemical assays demonstrate that, while exquisitely selective for caspase-6 over caspase-3 and -7, the compound's inhibitory activity is also dependent on the amino acid sequence and P1' character of the peptide substrate. The crystal structure of the ternary complex of caspase-6, substrate-mimetic and an 11 nM inhibitor reveals the molecular basis of inhibition. The general strategy to develop uncompetitive inhibitors together with the unique mechanism described herein provides a rationale for engineering caspase selectivity.

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عنوان ژورنال:

دوره 7  شماره 

صفحات  -

تاریخ انتشار 2012