Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation

摘要: Human serum albumin (HSA) is a target for reactive oxygen species (ROS), and alterations of its physiological functions caused by oxidation current issue. In this work, the amino-acid residues Trp-214 Lys-199, which are located at site I HSA, were experimentally computationally oxidized, effect on binding constant with phenylbutazone was measured. HSA submitted to two mild oxidizing reagents, taurine monochloramine (Tau-NHCl) dibromamine (Tau-NBr2). The provoked spectroscopic in protein consistent formation N′-formylkynurenine. It found that Tau-NBr2, but not Tau-NHCl, significant increase association phenylbutazone. Lys-199 modeled simulated changing these using putative products. Based Amber score function, interaction energy measured, it showed that, while native presented an −21.3 kJ/mol, altered N′-formylkynurenine resulted −28.4 carbonylated form −33.9 kJ/mol. summary, experimental theoretical findings show oxidative affect efficacy.