Understanding the based-on drug or drug conjugates to reach the beneficial optimally recognized by the immune system requires multidisciplinary approaches and detailed of albumin as the key circulating a transporting/transmission and antioxidant protein of blood drug interaction. Albumin, in reduced form (mercaptoalbumin, HMA), with antioxidant ability and alterations/deteriorations in the redox status of human serum albumin (HSA) under oxidative stress formation in infection diseases and its complications strongly modifies albumin antioxidant capacity. The aim of this study was the investigation of carbonyl/oxidative stress and pseudo-esterase activity of mercaptolbumin and oxidized HSA models. HSA (P. pastoris) purchased from MedChemExpress (USA) was used for study to model oxidative stress, HSA in reduced (intact) form was treated with H2O2, tert-butylhydroperoxide (t-BHP) and chloramine T (CT). The content of HSA-bound carbonyl groups decreased in under treatment with t-BPH- and CT-reduced HSA and more less extent in case of H2O2-treated. Fatty acid-free HSA and mercaptoalbumin (HMA) advanced oxidation protein products (AOPP) concentrations were significantly lower than in H2O2 loading reduced HSA by 123% and 235%, respectively. The total thiols level was lower in HMA + CT compared to reduced HMA by 51% and even increased after treatment of HMA with H2O2. Pseudo-esterase activity of HMA maintains >65% in the presence of hydroperoxide and occurs pronounced loss in the presence of chloramine T. Hydrogen peroxide at physiological concentration about 10 μM occurs less damage of reduced from of HSA then t-BPH and CT, and unlike t-BPH and CT, without significantly changes in pseudo-esterase activities.
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