15087-95-3Relevant academic research and scientific papers
One-Pot Telescoped Synthesis of Thiazole Derivatives from β-Keto Esters and Thioureas Promoted by Tribromoisocyanuric Acid
De Andrade, Vitor S. C.,De Mattos, Marcio C. S.
, p. 4867 - 4874 (2018)
A simple and efficient one-pot protocol has been developed for the synthesis of thiazole derivatives from readily available starting materials. Tribromoisocyanuric acid was successfully used for α-monohalogenation of β-keto esters in aqueous medium, which
Development of 2-(Substituted Benzylamino)-4-Methyl-1, 3-Thiazole-5-Carboxylic Acid Derivatives as Xanthine Oxidase Inhibitors and Free Radical Scavengers
Ali, Md Rahmat,Kumar, Suresh,Afzal, Obaid,Shalmali, Nishtha,Sharma, Manju,Bawa, Sandhya
, p. 508 - 516 (2016/03/19)
A series of 2-(substituted benzylamino)-4-methylthiazole-5-carboxylic acid was designed and synthesized as structural analogue of febuxostat. A methylene amine spacer was incorporated between the phenyl ring and thiazole ring in contrast to febuxostat in which the phenyl ring was directly linked with the thiazole moiety. The purpose of incorporating methylene amine was to provide a heteroatom which is expected to favour hydrogen bonding within the active site residues of the enzyme xanthine oxidase. The structure of all the compounds was established by the combined use of FT-IR, NMR and MS spectral data. All the compounds were screened in vitro for their ability to inhibit the enzyme xanthine oxidase as per the reported procedure along with DPPH free radical scavenging assay. Compounds 5j, 5k and 5l demonstrated satisfactory potent xanthine oxidase inhibitory activities with IC50 values, 3.6, 8.1 and 9.9 μm, respectively, whereas compounds 5k, 5n and 5p demonstrated moderate antioxidant activities having IC50 15.3, 17.6 and 19.6 μm, respectively, along with xanthine oxidase inhibitory activity. Compound 5k showed moderate xanthine oxidase inhibitory activity as compared with febuxostat along with antioxidant activity. All the compounds were also studied for their binding affinity in active site of enzyme (PDB ID-1N5X).
