1588-83-6Relevant articles and documents
Benzoic acid derivatives with trypanocidal activity: Enzymatic analysis and molecular docking studies toward trans-sialidase
Kashif, Muhammad,Moreno-Herrera, Antonio,Villalobos-Rocha, Juan Carlos,Nogueda-Torres, Benjamín,Pérez-Villanueva, Jaime,Rodríguez-Villar, Karen,Medina-Franco, José Luis,De Andrade, Peterson,Carvalho, Ivone,Rivera, Gildardo
, (2017/11/20)
Chagas, or American trypanosomiasis, remains an important public health problem in developing countries. In the last decade, trans-sialidase has become a pharmacological target for new anti-Chagas drugs. In this work, the aims were to design and find a new series of benzoic acid derivatives as trans-sialidase (TS) inhibitors and anti-trypanosomal agents. Three compounds (14, 18, and 19) sharing a para-aminobenzoic acid moiety showed more potent trypanocidal activity than the commercially available drugs nifurtimox and benznidazole in both strains: the lysis concentration of 50% of the population (LC50) was 0.15 μM on the NINOA strain, and LC50 0.22 μM on the INC-5 strain. Additionally, compound 18 showed a moderate inhibition (47%) on the trans-sialidase enzyme and a binding model similar to DANA (pattern A).
Synthesis and evaluation of alternative substrates for arginase
Han, Shoufa,Moore, Roger A.,Viola, Ronald E.
, p. 81 - 94 (2007/10/03)
Two novel carboxyl-containing arginase substrates, 4-guanidino-3-nitrobenzoic acid and 4-guanidino-2-nitrophenylacetic acid, have been synthesized and found to give enhanced catalysis and dramatically lower Km values relative to 1-nitro-3-guanidinobenzene, a substrate designed for use in a chromophoric arginase assay. To more efficiently mimic the natural substrate, a series of sulfur analogs of L-arginine were synthesized and kinetically characterized. The parent compound, L-thioarginine, with the bridging guanidinium nitrogen of L-arginine replaced with sulfur, functions as efficiently as the natural substrate. The desamino analog shows extremely low turnover, while the kcat of the descarboxy analog is only 75-fold lower than that of arginine. These results suggest that the bridging nitrogen of L-arginine is not important for either substrate binding or catalysis, while the α-carboxyl group facilitates substrate binding, and the α-amino group is necessary for efficient catalysis. Isothiourea homologs previously reported to be nitric oxide synthase inhibitors have been found to undergo a rapid non-enzymatic rearrangement to a species that is probably the true inhibitor.
1,1,1-trimethylhydrazinium iodide: A novel, highly reactive reagent for aromatic amination via vicarious nucleophilic substitution of hydrogen
Pagoria, Philip F.,Mitchell, Alexander R.,Schmidt, Robert D.
, p. 2934 - 2935 (2007/10/03)
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