67320-80-3Relevant academic research and scientific papers
Control of 6-Exo and 7-Endo cyclizations of alkynylamides using platinum and bismuth catalysts
Girard, Anne-Lise,Enomoto, Taro,Yokouchi, Shinsuke,Tsukano, Chihiro,Takemoto, Yoshiji
supporting information, p. 1321 - 1324 (2013/01/11)
The rules of cyclization: Alkynylamides are regioselectively cycloisomerized into piperazin-2-one and 1,4-diazepan-2-one derivatives by using catalytic amounts of appropriate metal catalysts. A 6-exo-dig addition proceeds in the presence of Bi(OTf)3, while the 7-endo-dig addition occurs with PtCl2 for the same substrate. (see scheme; Ns=o- nitrobenzenesulfonyl, Ts=p-toluenesulfonyl, Cbz=benzyloxycarbonyl, DCE=dichloroethane) Copyright
Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors
Ward, Yancey D.,Thomson, David S.,Frye, Leah L.,Cywin, Charles L.,Morwick, Tina,Emmanuel, Michel J.,Zindell, Renée,McNeil, Daniel,Bekkali, Younes,Giradot, Marc,Hrapchak, Matt,DeTuri, Molly,Crane, Kathy,White, Della,Pav, Susan,Wang, Yong,Hao, Ming-Hong,Grygon, Christine A.,Labadia, Mark E.,Freeman, Dorothy M.,Davidson, Walter,Hopkins, Jerry L.,Brown, Maryanne L.,Spero, Denice M.
, p. 5471 - 5482 (2007/10/03)
The specificity of the immune response relies on processing of foreign proteins and presentation of antigenic peptides at the cell surface. Inhibition of antigen presentation, and the subsequent activation of T-cells, should, in theory, modulate the immune response. The cysteine protease Cathepsin S performs a fundamental step in antigen presentation and therefore represents an attractive target for inhibition. Herein, we report a series of potent and reversible Cathepsin S inhibitors based on dipeptide nitriles. These inhibitors show nanomolar inhibition of the target enzyme as well as cellular potency in a human B cell line. The first X-ray crystal structure of a reversible inhibitor cocrystallized with Cathepsin S is also reported.
