Multi-Spectroscopic and Molecular Modeling Studies of Interactions Between Anionic Porphyrin and Human Serum Albumin.

The subject of this study is the interaction between 5,10,15,20-tetrakis (4-sulfonatophenyl)-porphyrin (TSPP), a potential photosensitizer for photodynamic therapy (PDT) and radiotherapy, and human serum albumin (HSA), a crucial protein in the body. The main objective was to investigate the binding mechanisms, structural changes, and potential implications of these interactions for drug delivery and therapeutic applications. Spectroscopic techniques and computational methods were employed to investigate the mechanism and effects of TSPP binding by HSA.

Aggregation of Albumins under Reductive Radical Stress.

The reactions of radicals with human serum albumin (HSA) under reductive stress conditions were studied using pulse radiolysis and photochemical methods. It was proved that irradiation of HSA solutions under reductive stress conditions results in the formation of stable protein aggregates. HSA aggregates induced by ionizing radiation are characterized by unique emission, different from the UV emission of non-irradiated solutions.

Human serum albumin as a potential drug delivery system for N-methylated hot spot insulin analogs inhibiting hormone aggregation.

The purpose of this study was to investigate whether Human Serum Albumin (HSA) can bind N-methylated analogs of hot spots of native insulin. Three N-methylated derivatives of the A13-A19 fragment of native insulin were used: L(N-Me)YQLENY (1), LYQ(N-Me)LENY (2), and L(N-Me)YQ(N-Me)LENY (3). The studied N-methylated insulin fragments possess inhibiting potential against hormone aggregation.

Influence of Ionizing Radiation on Spontaneously Formed Aggregates in Proteins or Enzymes Solutions.

We have shown that many proteins and enzymes (ovalbumin, β-lactoglobulin, lysozyme, insulin, histone, papain) undergo concentration-dependent reversible aggregation as a result of the interaction of the studied biomolecules. Moreover, irradiation of those protein or enzyme solutions under oxidative stress conditions results in the formation of stable soluble protein aggregates. We assume that protein dimers are mainly formed.

Fullerenol C(OH) Protects the Antioxidant Enzymes in Human Erythrocytes against Oxidative Damage Induced by High-Energy Electrons.

Ionizing radiation (IR) can pass through the human body easily, potentially causing severe damage to all biocomponents, which is associated with increasing oxidative stress. IR is employed in radiotherapy; however, in order to increase safety, it is necessary to minimize side effects through the use of radioprotectors. Water-soluble derivatives of fullerene exhibit antiradical and antioxidant properties, and these compounds are regarded as potential candidates for radioprotectors.

Spontaneous and Ionizing Radiation-Induced Aggregation of Human Serum Albumin: Dityrosine as a Fluorescent Probe.

The use of spectroscopic techniques has shown that human serum albumin (HSA) undergoes reversible self-aggregation through protein−protein interactions. It ensures the subsequent overlapping of electron clouds along with the stiffening of the conformation of the interpenetrating network of amino acids of adjacent HSA molecules. The HSA oxidation process related to the transfer of one electron was investigated by pulse radiolysis and photochemical methods.

Synthesis and Properties of Targeted Radioisotope Carriers Based on Poly(Acrylic Acid) Nanogels.

Radiation crosslinking was employed to obtain nanocarriers based on poly(acrylic acid)-PAA-for targeted delivery of radioactive isotopes. These nanocarriers are internally crosslinked hydrophilic macromolecules-nanogels-bearing carboxylic groups to facilitate functionalization. PAA nanogels were conjugated with an engineered bombesin-derivative-oligopeptide combined with 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetate chelating moiety, aimed to provide selective radioligand transport.

Dynamics of Ion Pairing in Dilute Aqueous HCl Solutions by Spectroscopic Measurements of Hydroxyl Radical Conversion into Dichloride Radical Anions.

The rate of formation of dichloride anions (Cl) in dilute aqueous solutions of HCl (2-100 mmol·kg) was measured by the technique of pulse radiolysis over the temperature range of 288-373 K. The obtained Arrhenius dependence shows a concentration averaged activation energy of 7.3 ± 1.

Human Serum Albumin Binds Native Insulin and Aggregable Insulin Fragments and Inhibits Their Aggregation.

The purpose of this study was to investigate whether Human Serum Albumin (HSA) can bind native human insulin and its A13-A19 and B12-B17 fragments, which are responsible for the aggregation of the whole hormone. To label the hormone and both hot spots, so that their binding positions within the HSA could be identified, 4-(1-pyrenyl)butyric acid was used as a fluorophore. Triazine coupling reagent was used to attach the 4-(1-pyrenyl)butyric acid to the N-terminus of the peptides.

Ionic-Equilibrium-Based Mechanism of OH Conversion to Dichloride Radical Anion in Aqueous Acidic Solutions by Kinetic and Theoretical Studies.

A new mechanism for the dichloride radical anion (Cl) formation in diluted acidic chloride solutions is proposed on the grounds of pulse radiolysis measurements of the optical absorption growth at 340 nm and the density functional theory and Hartree-Fock computations. We show that the rate of OH conversion into Cl is determined by the equilibrium concentration of the ionic pair HO·Cl. According to the proposed mechanism, the diffusional encounter of OH and HO·Cl is followed by fast concerted charge/proton transfer ( k(25 °C) = 6.

Fullerenol C(OH) protects human erythrocyte membrane against high-energy electrons.

Fullerenols (polyhydroxylated fullerene C) are nanomaterial with potentially broad applicability in biomedical sciences with high antioxidant ability, thus, we investigated the radioprotecting potential of fullerenol C(OH) on human erythrocytes irradiated by high-energy electrons of 6 MeV. The results demonstrate that C(OH) at concentration of 150 μg/mL protects the erythrocytes against the radiation-induced hemolysis (comparing to non-protected cells, we observed 30% and 39% protection for 0.65 and 1.

Interaction of cationic protoberberine alkaloids with human serum albumin. No spectroscopic evidence on binding to Sudlow's site 1.

Physicochemical studies on drug interactions with human serum albumin (HSA) are relevant for elucidation, at the molecular level, of the processes occurring in vivo. In this work using optical spectroscopic methods (fluorescence, absorption, circular dichroism), we have investigated aqueous HSA solutions containing pharmaceutically important isoquinoline alkaloids, berberine and palmatine. The primary objective was to verify whether the two compounds are located in the subdomain IIA of the secondary HSA structure as reported in literature.

Aggregation of perfluoropolyether carboxylic salts in aqueous solutions. Fluorescence probe study.

Aqueous solutions of anionic surfactants Cl(C3F6O)nCF2COOX, consisting of n = 2 and 3 perfluoroisopropoxy units and the counterion X = Na+ or NH4+, were studied by the method of fluorescence quenching with the use of (1-pyrenylbutyl)trimethylammonium bromide as a luminophore, and 1,1'-dimethyl-4,4'bipyridinium dichloride (methyl viologen) as a quencher. From the kinetics of fluorescence decay (time-resolved experiments) micellar aggregation numbers, N, and rate constants of the intramicellar quenching were determined for a wide range of surfactant concentrations, on the basis of the model developed by Infelta and Tachiya. The results are discussed in terms of the shape of the aggregates and the degree of counterion binding.

In vitro antileukemic, antioxidant and prooxidant activities of Antoksyd S (C/E/XXI): a comparison with baicalin and baicalein.

There is increasing interest concerning the use of natural antioxidants as low toxic antileukemic compounds. Antoksyd S (C/E/XXI), is a novel herbal drug derived in Poland from the powdered roots of Scutellaria baicalensis, and the biological activities of its major components (baicalin and baicalein) were compared on the human leukemia cell line HL-60. On MTT assay, Antoksyd S (C/E/XXI) showed an obvious cytotoxic effect on HL-60 cells, which was compared with those caused by cisplatin and doxorubicin under the same experimental conditions.