27243-15-8Relevant articles and documents
Protein assembly directed by synthetic molecular recognition motifs
Ma, Mingming,Bong, Dennis
, p. 7296 - 7299 (2011)
Tris-functionalized cyanuric acid (TCA) and melamine (TM) selectively recognize each other in aqueous solution with 1:1 stoichiometry. We have coupled biotin to TCA and TM to allow pseudo-tetrahedral display of TCA and TM on streptavidin through biotin-ligand binding. Synthetic cyanuric acid/melamine recognition is found to drive selective protein-protein assembly.
Synthesis and Tritium Labelling of 6β-Amino-4,5α-epoxymorphinans and Their 14-Hydroxy Derivatives as Potential Affinity Labelling Probes with μ Opioid Agonist Activity
Oetvoes, Ferenc,Toth, Geza,Lovas, Sandor,Simon, Csaba,Hosztafi, Sandor
, p. 133 - 136 (1996)
The synthesis of 6β-(methylfumaramido) and 6β-chloroacetamido derivatives 1b and 1c of 6β-amino-7,8-didehydromorphinan and the corresponding 14-hydroxy derivatives 1e and 1f are described.The 7,8-dihydro derivatives of these compounds were synthesized in inactive (2b,c,e,f) as well as in tritiated form (3b,c,e,f).
Therapeutic targeting of oncogenic K-ras by a covalent catalytic site inhibitor
Lim, Sang Min,Westover, Kenneth D.,Ficarro, Scott B.,Harrison, Rane A.,Choi, Hwan Geun,Pacold, Michael E.,Carrasco, Martin,Hunter, John,Kim, Nam Doo,Xie, Ting,Sim, Taebo,Jaenne, Pasi A.,Meyerson, Matthew,Marto, Jarrod A.,Engen, John R.,Gray, Nathanael S.
supporting information, p. 199 - 204 (2014/01/17)
We report the synthesis of a GDP analogue, SML-8-73-1, and a prodrug derivative, SML-10-70-1, which are selective, direct-acting covalent inhibitors of the K-Ras G12C mutant relative to wild-type Ras. Biochemical and biophysical measurements suggest that modification of K-Ras with SML-8-73-1 renders the protein in an inactive state. These first-in-class covalent K-Ras inhibitors demonstrate that irreversible targeting of the K-Ras guanine-nucleotide binding site is potentially a viable therapeutic strategy for inhibition of Ras signaling. Putting a stop to Ras: Two new selective, direct-acting covalent inhibitors of the K-Ras G12C mutant are reported. Studies suggest that the modification of K-Ras with SML-8-73-1 renders the protein inactive. These novel covalent inhibitors demonstrate that irreversible targeting of the K-Ras guanine-nucleotide binding site is potentially a viable therapeutic strategy for inhibition of Ras signaling. Copyright
Synthesis, biological evaluation, and structure-activity relationships of potent noncovalent and nonpeptidic cruzain inhibitors as anti-Trypanosoma cruzi agents
Ferreira, Rafaela S.,Dessoy, Marco A.,Pauli, Ivani,Souza, Mariana L.,Krogh, Renata,Sales, Ana I. L.,Oliva, Glaucius,Dias, Luiz C.,Andricopulo, Adriano D.
supporting information, p. 2380 - 2392 (2014/04/17)
The development of cruzain inhibitors has been driven by the urgent need to develop novel and more effective drugs for the treatment of Chagas' disease. Herein, we report the lead optimization of a class of noncovalent cruzain inhibitors, starting from an inhibitor previously cocrystallized with the enzyme (Ki = 0.8 μM). With the goal of achieving a better understanding of the structure-activity relationships, we have synthesized and evaluated a series of over 40 analogues, leading to the development of a very promising competitive inhibitor (8r, IC50 = 200 nM, Ki = 82 nM). Investigation of the in vitro trypanocidal activity and preliminary cytotoxicity revealed the potential of the most potent cruzain inhibitors in guiding further medicinal chemistry efforts to develop drug candidates for Chagas' disease.
