L-trans-Epoxysuccinyl-Leu-4-guanidinobutylamide

An irreversible, highly selective cysteine protease inhibitor. Shows no inhibition against serine proteases with an except of trypsin. Interacts with the Sn subsites of proteases. For in vivo studies the use of E-64 as a cysteine protease inhibitor is highly recommanded because it has a specific inhibition, it is permeable in cells and tissues and has low toxicity. Inhibits activation-induced programmed cell death and restores defective immune responses in HIV+ donors Potential targets: Papain, Bromelain, Ficin, Cathepsin B, H and L, Tumor-Cathepsin, Calpain References: K. Hanada, M. Tamai, M. Yamagishi, S.Ohmura, J. Sawada & I. Tanaka (1978) Isolation and Characterization of E-64, a New Thiol Protease Inhibitor. Agric. Bioi. Chem., 42 (3), 523-­528. A. J. Barrett, A. A. Kembhavi, M. A. Brown, H. Kirschke, C. G. Knight, M. Tamai, K. Hanada (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J., 201(1), 189­98. K. Matsumoto, K. Mizoue, K. Kitamura, W. C. Tse, C. P. Huber, T. Ishida (1999) Structural basis of inhibition of cysteine proteases by E-64 and its derivatives. Biopolymers, 51(1), 99­107.