scholarly journals Study on the interaction of Prodigiosin with bovine serum albumin by spectroscopic methods

2012 ◽  
Vol 27 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Shu-Chao Liu ◽  
Jing Tang ◽  
Xi-Hai Zhang ◽  
Yuan-Yuan Gao ◽  
Fei Ma ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Synchronous Fluorescence ◽  
Spectroscopic Methods ◽  
Amino Acid Residues ◽  
Absorption And Fluorescence Spectra ◽  
Ft Ir ◽  
Spectrum Experiment

The interaction between bovine serum albumin (BSA) and Prodigiosin (PG) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, FT-IR and circular dichroism (CD) techniques. The data of UV-vis absorption and fluorescence spectra displayed that there existed interaction between PG and aromatic amino acid residues of BSA. The synchronous fluorescence and CD spectrum experiment both showed that the secondary structure of BSA changed with addition of PG. All these results revealed that the conformation and microenvironment of BSA were changed.

Research on the Interaction between Pheophorbide and Bovine Serum Albumin

2013 ◽  
Vol 749 ◽  
pp. 471-476 ◽  
Author(s):  
Yong Ye ◽  
Xue Lan Chen ◽  
Ya Guo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Serum Protein ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Synchronous Fluorescence ◽  
Tryptophan Residue ◽  
Hydrophobic Force ◽  
Synchronous Fluorescence Spectra ◽  
Spontaneous Interaction

The interaction between natural pheophorbide (a superior photosensitizer) and bovine serum albumin (BSA) in physiological condition is investigated by means of UV-Vis, fluorescence and synchronous fluorescence spectra so as to provide the basis for clinical use. Natural pheophorbide was isolated from silkworm excrement. BSA in pH 7.4 Tris buffer mixed with different concentration of pheophorbide was kept at certain temperature for 3 h or under illumination by laser at 630 nm for 20 min. UV-Vis absorption of BSA was enhanced and its fluorescence was quenched by pheophorbide. Illumination of laser at 630 nm intensified the quenching. The mechanism is deemed as mainly static quenching. The binding constants Ka at 300, 310, 320 K are separately 6.93×1012,7.40×1012,6.82×1012 L/mol/s respectively. Number of binding sites n is 1; the binding distance R is 3.70 nm, and that suggests non-radiation energy transfer from BSA to pheophorbide. The thermodynamic parameters of the binding reaction are H=36.7 kJ/mol, S=213 J/mol/K, and G negative value, and indicates that hydrophobic force plays a predominant role in the process, and it is a spontaneous interaction. Synchronous fluorescence spectra show that pheophorbide mainly interacts with tryptophan residue of BSA and leads to the promotion of hydrophobic force. Pheophorbide can bind to serum protein and be transported in vivo, makes no destruction to molecular structure of serum protein, but causes its conformational alteration.

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS

2021 ◽  
Author(s):  
Olesya Viktorovna Pokidova ◽  
◽  
Nina Sergeevna Emel’yanova ◽  
Alexander Vasilievich Kulikov ◽  
Alexander Ivanovich Kotelnikov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Reduced Glutathione ◽  
Decay Product ◽  
Iron Complex ◽  
Amino Acid Residues ◽  
Cationic Complex ◽  
Nitrosyl Iron Complex

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

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