76684-89-4Relevant academic research and scientific papers
Design, synthesis, and screen of cathepsin K inhibitors
Yu, Ying-Ying,Sun, Wei,Dong, Lei,Liu, Hai-Dong,Jiang, Dan,Xiao, Jun-Hai,Yang, Xiao-Hong,Li, Song
, p. 715 - 718 (2013/07/26)
We synthesized a series of epoxysuccinic acid derivatives and evaluated their in vitro cathepsin K inhibitory activity The screening results show that the potency of compounds 9e, 9d, 9p, 9j and 9k (IC50 ≤ 0.005 μmol/L) were equal to or greater than that of the lead compound 9a. Less hydrophobic compounds showed weaker potency, which can be explained by the hydrophobic nature of the cathepsin K binding pockets.
Stereoselective synthesis of the epoxysuccinyl peptide E-64c
Lygo, Barry,Gardiner, Stuart D.,To, Daniel C. M.
, p. 2063 - 2066 (2008/02/05)
A highly diastereoselective PTC epoxidation is employed in the synthesis of the potent cysteine protease inhibitor E-64c. Georg Thieme Verlag Stuttgart.
Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
Meara, Joseph P.,Rich, Daniel H.
, p. 3357 - 3366 (2007/10/03)
Analogs of the epoxysuccinyl peptide cysteine proteinase inhibitor, EP- 475 (2a), in which the free carboxylate has been replaced by hydroxamic acid, amide, methyl ketone, hydroxyl, and ethyl ester functionalities, have been synthesized. Individual rate c
Ester and amide derivatives of E64c as inhibitors of platelet calpains
Huang,McGowan,Detwiler
, p. 2048 - 2054 (2007/10/02)
Ester and amide derivatives of E64c, (+)-(2S,3S)-3-[[(S)-3-methyl-1-[(3- methylbutyl)carbamoyl]butyl]carbamoyl]-2-oxiranecarboxylic acid, an inhibitor of calpains, were synthesized and tested for ability to inhibit calpain in lysed cells, ability to enter
