915796-93-9Relevant articles and documents
Synthesis and evaluation of peptidic irreversible inhibitors of tissue transglutaminase
Pardin, Christophe,Gillet, Steve M.F.G.,Keillor, Jeffrey W.
, p. 8379 - 8385 (2006)
Herein we report the synthesis and the evaluation of eight novel compounds as irreversible inhibitors of transglutaminase (TGase). These compounds are based on a minimal peptidic scaffold shown previously [Chem. Biol. 2005, 12, 469-475] to confer affinity for the TGase active site and bear electrophilic groups such as α,β-unsaturated amide, chloroacetamide or maleimide; their general structure being Cbz-Phe-spacer-electrophile. The affinity conferred by the Cbz-Phe scaffold was determined by comparison to N-propylacrylamide and the length of the spacer was also varied to evaluate its importance. The inhibitory efficiencies (kinact/KI) of these compounds vary up to 105 M-1 min-1, among the highest reported for derivatives based on this simple Cbz-Phe peptidic scaffold.
