scholarly journals INTERACTION OF COPPER OXIDE NANOPARTICLES WITH BOVINE SERUM ALBUMIN BY SPECTROSCOPIC STUDIES

2018 ◽  
Vol 10 (5) ◽  
pp. 35
Author(s):  
Suja Abraham ◽  
Vellaichamy Parthasarathy
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Intensity ◽  
Bovine Serum ◽  
Structural Changes ◽  
Fluorescence Emission ◽  
Average Particle ◽  
Time Resolved ◽  
Cuo Nps ◽  
Fluorescence Measurements

Objective: Since structural changes of adsorbed protein are necessary for cellular uptake of nanoparticles (NPs) it is of prime importance to know about structural changes of bovine serum albumin (BSA) when it interacts with CuO NPs–a potential new antitumor drug.Methods: CuO NPs prepared by sol-gel technique were characterized by x-ray diffraction (XRD) and tunneling electron microscope (TEM) techniques. The conformational changes induced by CuO NPs on BSA were studied by various spectroscopic techniques such as steady state and time-resolved fluorescence measurements. The changes in fluorescence emission parameters such as fluorescence intensity, fluorescence emission maximum and lifetimes of fluorescent residues in BSA were studied.Results: XRD analysis showed the average particle size as 32 nm. The TEM micrograph showed particles of different size varying from 10 to 45 nm. Fluorescence quenching was confirmed due to a decrease in fluorescence intensity of CuO NPs–BSA complex. The analysis of lifetime measurements indicated BSA contained two tryptophan (trp) residues that fluoresced in different environments. Static quenching mechanism was confirmed by time-resolved measurements when BSA interacted with CuO NPs.Conclusion: Minor structural changes of BSA protein were observed during the interaction studies.

scholarly journals Radioprotective Role of Vitamins C and E against the Gamma Ray-Induced Damage to the Chemical Structure of Bovine Serum Albumin

Antioxidants ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1875
Author(s):  
Hajar Zarei ◽  
Mostean Bahreinipour ◽  
Yahya Sefidbakht ◽  
Shokouh Rezaei ◽  
Rouhollah Gheisari ◽  
...  
Keyword(s):  
Vitamin E ◽  
Bovine Serum Albumin ◽  
Vitamin C ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Changes ◽  
Gamma Ray ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Radiation Induced

Radioprotective effects of vitamin C and vitamin E as a water-soluble and a lipid-soluble agent, respectively, were investigated at the molecular level during the imposition of gamma radiation-induced structural changes to bovine serum albumin (BSA) at the therapeutic dose of 3 Gy. Secondary and tertiary structural changes of control and irradiated BSA samples were investigated using circular dichroism and fluorescence spectroscopy. The preirradiation tests showed nonspecific and reversible binding of vitamins C and E to BSA. Secondary and tertiary structures of irradiated BSA considerably changed in the absence of the vitamins. Upon irradiation, α-helices of BSA transitioned to beta motifs and random coils, and the fluorescence emission intensity decreased relative to nonirradiated BSA. In the presence of the vitamins C or E, however, the irradiated BSA was protected from these structural changes caused by reactive oxygen species (ROS). The two vitamins exhibited different patterns of attachment to the protein surface, as inspected by blind docking, and their mechanisms of protection were different. The hydrophilicity of vitamin C resulted in the predominant scavenging of ROS in the solvent, whereas hydrophobic vitamin E localized on the nonpolar patches of the BSA surface, where it did not only form a barrier for diffusing ROS but also encountered them as an antioxidant and neutralized them thanks to the moderate BSA binding constant. Very low concentrations of vitamins C or E (0.005 mg/mL) appear to be sufficient to prevent the oxidative damage of BSA.

Influence of metal ions on thermal aggregation of bovine serum albumin: Aggregation kinetics and structural changes

2009 ◽  
Vol 103 (12) ◽  
pp. 1729-1738 ◽  
Author(s):  
Giovanna Navarra ◽  
Anna Tinti ◽  
Maurizio Leone ◽  
Valeria Militello ◽  
Armida Torreggiani
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Structural Changes ◽  
Aggregation Kinetics ◽  
Thermal Aggregation

Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd(II) complex incorporating 2,2′-(propane-1,3-diyl)bis(1H-imidazole-4,5-dicarboxylate)

2019 ◽  
Vol 44 (3-4) ◽  
pp. 198-205 ◽  
Author(s):  
Xiao-Fei Li ◽  
Li-Gang Ma ◽  
Yan-Qiu Yang ◽  
Yan-Ju Liu ◽  
Xiang-Ru Meng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Entropy Change ◽  
Chain Structure ◽  
Binding Studies ◽  
Carboxylate Oxygen ◽  
Fluorescence Measurements ◽  
Bovine Serum Albumin Binding

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.

scholarly journals Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

2013 ◽  
Vol 36 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol-Khalegh Bordbar ◽  
Yadolahe Khodadusdt
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Conformation ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Aggregate Formation ◽  
Cationic Porphyrin ◽  
Porphyrin Complex ◽  
Induced Aggregation

The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

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