143978-92-1Relevant articles and documents
Isoselenocyanates derived from Boc/Z-amino acids: Synthesis, isolation, characterization, and application to the efficient synthesis of unsymmetrical selenoureas and selenoureidopeptidomimetics
Chennakrishnareddy, Gundala,Nagendra, Govindappa,Hemantha, Hosahalli P.,Das, Ushati,Guru Row, Tayur N.,Sureshbabu, Vommina V.
supporting information; experimental part, p. 6718 - 6724 (2010/09/30)
Isoselenocyanates derived from Boc/Z-amino acids are prepared by the reaction of the corresponding isonitriles with selenium powder in presence of triethylamine at reflux. The utility of these new classes of isoselenocyanates in the preparation of selenoureidodipeptidomimetics possessing both amino as well as carboxy termini has been accomplished. The 1H NMR analysis confirmed that the protocol involving the conversion of isonitriles to isoselenocyanates and their use as coupling agents in assembling selenoureido derivatives is free from racemization.
Synthesis of Boc-amino tetrazoles derived from α-amino acids
Sureshbabu, Vommina V.,Naik, Shankar A.,Nagendra
experimental part, p. 395 - 406 (2009/06/06)
A simple route for the synthesis of Boc-protected tetrazole analogs of amino acids starting from Nα-Boc amino acids has been described. The [2 + 3] cycloaddition of Boc-α-amino nitrile and sodium azide in the presence of a catalytic amount of zinc bromide yielded the desired tetrazoles in good yields and purity. All the compounds obtained have been characterized by 1H and 13C-NMR and mass spectral studies. Copyright Taylor & Francis Group, LLC.
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.
