ABSTRACT
The generation of hydroxyl radicals from hydrogen peroxide in aqueous solutions containing magnetic nanoparticles (MNPs), hemoglobin (Hb), immunoglobulin G (IgG), and human serum albumin (HSA) was determined. The dependence of the rate of formation of the oxidized product of o-phenylenediamine (o-PDA) on the concentration of MNPs in solution, as well as on the concentration of proteins, was obtained. The peroxidase-like activity of MNPs was shown to decrease in the presence of HSA and IgG, while the addition of Hb to the reaction mixture led to its decrease and increase depending on protein concentration. The obtained effects can be used in the engineering of systems based on MNPs for theranostics (in particular, for suppression of tumor growth) and in predicting the ability of particles to catalyze the generation of reactive oxygen species (ROS) in vivo.
Subject(s)
Magnetite Nanoparticles , Nanoparticles , Humans , Reactive Oxygen Species , Blood Proteins , Hydrogen Peroxide , Hemoglobins , Immunoglobulin G , PeroxidasesABSTRACT
For the first time, with the aid of differential scanning calorimetry, the thermal denaturation of fibrinogen under induced oxidation was studied. All fibrinogen structural elements detected by DSC (D region, αC-domain, and E region) are subjected to oxidation. Structural changes in fibrinogen molecule were characterized by the denaturation temperature, denaturation enthalpy, and van't Hoff enthalpy.
Subject(s)
Fibrinogen/chemistry , Protein Processing, Post-Translational , Calorimetry, Differential Scanning/methods , Humans , Oxidation-Reduction , Protein DomainsABSTRACT
For the first time, by using the complex of physicochemical methods (mass-spectrometry, differential scanning calorimetry, spectrofluorimetry, method of spectral and fluorescent probes, dynamic light scattering, and UV spectrophotometry), the oxidation-mediated modification of chemical and spatial structure of albumin has been studied. All albumin structural regions are subjected to oxidation, methionine and aromatic amino acids primarily involved in oxidation. The albumin melting shows a decrease in thermal stabilization of the structure and changing of aggregation upon oxidation. The change in physical and chemical properties of albumin under different quantity of the oxidizer has been analyzed.
Subject(s)
Serum Albumin/metabolism , Amino Acid Sequence , Humans , Models, Molecular , Oxidation-Reduction , Ozone/metabolism , Protein Structure, Secondary , Serum Albumin/chemistryABSTRACT
The effect on ozone-induced oxidation on the self-assembly of fibrin in the presence of fibrin-stabilizing factor FXIIIa of soluble cross-linked fibrin oligomers was studied in a medium containing moderate urea concentrations. It is established that fibrin oligomers were formed by the protofibrils cross-linked through γ-γ dimers and the fibrils additionally cross-linked by through α-polymers. The oxidation promoted both the accumulation of greater amounts of γ-γ dimers and the formation of protofibrils, fibrils, and their dissociation products emerging with increasing urea concentrations, which have a high molecular weight. It is concluded that the oxidation enhances the axial interactions between D-regions of fibrin molecules.
