Molins-Molina, Oscar published the artcilePhotobinding of triflusal to human serum albumin investigated by fluorescence, proteomic analysis, and computational studies, Application In Synthesis of 328-90-5, the publication is Frontiers in Pharmacology (2019), Consuelo 1028, database is CAplus and MEDLINE.
Triflusal is a platelet antiaggregant employed for the treatment and prevention of thromboembolic diseases. After administration, it is biotransformed into its active metabolite, the 2-hydroxy-4-trifluoromethylbenzoic acid (HTB). We present here an investigation on HTB photobinding to human serum albumin (HSA), the most abundant protein in plasma, using an approach that combines fluorescence, MS/MS, and peptide fingerprint anal. as well as theor. calculations (docking and mol. dynamics simulation studies). The proteomic anal. of HTB/HSA photolyzates shows that HTB addition takes place at the e-amino groups of the Lys137, Lys199, Lys205, Lys351, Lys432, Lys525, Lys541 and Lys545 residues and involves replacement of the trifluoromethyl moiety of HTB with a new amide function. Only Lys199 is located in an internal pocket of the protein, and the remaining modified residues are placed in the external part. Docking and mol. dynamic simulation studies reveal that HTB supramol. binding to HSA occurs in the “V-cleft” region and that the process is assisted by the presence of Glu/Asp residues in the neighborhood of the external Lys, in agreement with the exptl. observed modifications. In principle, photobinding can occur with other trifluoroarom. compounds and may be responsible for the appearance of undesired photoallergic side effects.
Frontiers in Pharmacology published new progress about 328-90-5. 328-90-5 belongs to alcohols-buliding-blocks, auxiliary class Trifluoromethyl,Fluoride,Carboxylic acid,Benzene,Phenol, name is 2-Hydroxy-4-(trifluoromethyl)benzoic acid, and the molecular formula is C8H5F3O3, Application In Synthesis of 328-90-5.
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