1022-31-7Relevant articles and documents
A new mechanism of the photochemical oxidation of tryptophan sensitised with the uranyl ion
Ostakhov, Sergey S.,Kazakov, Valerii P.,Osina, Irina O.
, p. 113 - 114 (2009)
It has been found that tryptophan oxidation sensitised with the uranyl ion occurs as a chain reaction of Trp+ cation radicals with O2.
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Saito,I.,Matsuura,T.,Inoue,K.
, p. 188 (1981)
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Dye-sensitized Photo-oxygenation of Tryptophan to give N'-Formylkynurenine
Nakagawa, Masako,Kato, Shiro,Nakano, Kumiko,Hino, Tohru
, p. 855 - 856 (1981)
Exclusive conversion of the tricyclic hydroperoxide (1) into N'-formylkynurenine (2) has been found to occur in Na2CO3-AcOH (pH 7) and the methylene blue-sensitized photo-oxygenation of tryptophan in the same system has given N'-formylkynurenine as the sole product, in contrast with the reaction in water, which gave compound (1).
Formation of fluorophores from the kynurenine pathway metabolite N-formylkynurenine and cyclic amines involves transamidation and carbon-carbon bond formation at the 2-position of the amine
Tomek, Petr,Palmer, Brian D.,Kendall, Jackie D.,Flanagan, Jack U.,Ching, Lai-Ming
, p. 1772 - 1780 (2015)
Background Tryptophan catabolism along the kynurenine pathway is associated with a number of pathologies including cataract formation and cancer. Whilst the chemical reactions of kynurenine are well studied, less is known about the reactivity of its precu
Nitrobenzofurazan derivatives of N′-hydroxyamidines as potent inhibitors of indoleamine-2,3-dioxygenase 1
Paul, Saurav,Roy, Ashalata,Deka, Suman Jyoti,Panda, Subhankar,Trivedi, Vishal,Manna, Debasis
, p. 364 - 375 (2016/06/13)
Tryptophan metabolism through the kynurenine pathway is considered as a crucial mechanism in immune tolerance. Indoleamine 2,3-dioxygenase 1 (IDO1) plays a key role in tryptophan catabolism in the immune system and it is also considered as an important therapeutic target for the treatment of cancer and other diseases that are linked with kynurenine pathway. In this study, a series of nitrobenzofurazan derivatives of N′-hydroxybenzimidamides (1) and N′-hydroxy-2-phenylacetimidamides (2) were synthesized and their inhibitory activities against human IDO1 enzyme were tested using in-vitro and cellular enzyme activity assay. The optimization leads to the identification of potent compounds, 1d, 2i and 2k (IC50 = 39-80 nM), which are either competitive or uncompetitive inhibitors of IDO1 enzyme. These compounds also showed IDO1 inhibition potencies in the nanomolar range (IC50 = 50-71 nM) in MDA-MB-231 cells with no/negligible amount of cytotoxicity. The stronger selectivity of the potent compounds for IDO1 enzyme over tryptophan 2,3-dioxygenase (TDO) enzyme (312-1593-fold) also makes them very attractive for further immunotherapeutic applications.