scholarly journals Study on the Interaction of Bovine Serum Albumin with Ceftriaxone and the Inhibition Effect of Zinc (II)

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoli Yue ◽  
Tongfei Shen ◽  
Changna Wang ◽  
Chaohui Gao ◽  
Jifeng Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interactions ◽  
Binding Sites ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Uv Absorption ◽  
Inhibition Effect ◽  
Bsa Binding ◽  
Number Of Binding Sites

The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone with and without zinc (II) (Zn2+) was studied employing fluorescence, ultraviolet (UV) absorption, circular dichroism (CD), and synchronous fluorescence spectral methods. The intrinsic fluorescence of BSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmer calculations. The binding constant, the number of binding sites, and the thermodynamic parameters were obtained, which indicated a spontaneous and hydrophobic interaction between BSA and ceftriaxone regardless of Zn2+. Changes in UV absorption, CD, and synchronous fluorescence spectral data are due to the microenvironment of amide moieties in BSA molecules. In the BSA-ceftriaxone-Zn2+ system, Zn2+ must first interact with ceftriaxone forming a complex, which inhibits BSA binding to ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA and ceftriaxone in the presence and absence of Zn2+. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation.

scholarly journals Binding characteristics of reduced hepatic receptors for acetylated low-density lipoprotein and maleylated bovine serum albumin

1990 ◽  
Vol 265 (3) ◽  
pp. 689-698 ◽  
Author(s):  
E Ottnad ◽  
D P Via ◽  
H Sinn ◽  
E Friedrich ◽  
R Ziegler ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Binding Characteristics ◽  
Bsa Binding ◽  
35 Kda Protein

The binding characteristics of reduced hepatic membrane proteins for acetylated low-density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) have been examined. Two receptor activities were extracted from hepatic membranes in the presence of octyl beta-D-glucoside and beta-mercaptoethanol, and were separated by chromatography on Mal-BSA-Sepharose 4B. The receptors were revealed by ligand blotting. The active binding proteins had apparent molecular masses of 35 and 15 kDa in SDS/polyacrylamide gels. Equilibrium studies with protein-phosphatidylcholine complexes indicated that the reduced 35 kDa protein expresses two binding sites for Mal-BSA and one for acetyl-LDL, whereas the 15 kDa protein-phosphatidylcholine complex binds 131I-Mal-BSA and 131I-acetyl-LDL with a 4:1 stoichiometry. 131I-Mal-BSA binding was linear with both proteins, with a Kd of 4.8 nM at the 35 kDa protein and a Kd of 5.6 nM at the 15 kDa protein. The 35 kDa protein displayed saturable binding of 131I-acetyl-LDL with a Kd of 5 nM; the 15 kDa binding protein bound 131I-acetyl-LDL with a Kd of 2.3 nM. A 85 kDa protein was obtained by Mal-BSA-Sepharose chromatography when the hepatic membranes had been solubilized with Triton X-100 in presence of GSH/GSSG. This protein displayed saturable 131I-Mal-BSA binding with a Kd of 30 nM and 131I-acetyl-LDL binding with a Kd of 6.5 nM. The 131I-Mal-BSA binding capacity was four times higher than that of 131I-acetyl-LDL. Competition studies with the 35 kDa, 15 kDa and 85 kDa proteins binding Mal-BSA, acetyl-LDL, formylated albumin and polyanionic competitors provide evidence for the existence of more than one class of binding sites at the reduced binding proteins.

scholarly journals Complexation Peculiarities in “Doxorubicin–Bovine Serum Albumin–Gold Nanoparticles” Heterosystem. The Fluo-rescence Study

2020 ◽  
Vol 65 (6) ◽  
pp. 468
Author(s):  
N. A. Goncharenko ◽  
O. P. Dmytrenko ◽  
O. L. Pavlenko ◽  
M. P. Kulish ◽  
I. P. Pundyk ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Binding Sites ◽  
Binding Constant ◽  
Bovine Serum ◽  
Fluo Rescence ◽  
Number Of Binding Sites

The fluorescence (FL) quenching in aqueous solutions of doxorubicin (DOX)–bovine serum albumin (BSA)–gold nanoparticles (AuNPs) is studied. The existence of additional mechanisms of DOX-BSA complex formation leading to an increase in the binding constant K and a decrease in the number of binding sites n and the distance between the fluorophore and energy acceptors due to the presence of gold nanoparticles is shown.

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

2012 ◽  
Vol 554-556 ◽  
pp. 1678-1681 ◽  
Author(s):  
Yu Fen Liu ◽  
Hai Tao Xia ◽  
De Fu Rong
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Binding Constants ◽  
Gibbs Free Energy Change ◽  
Binding Reaction ◽  
Physiological Conditions ◽  
Number Of Binding Sites

The binding reaction of Zn(II) complex [Zn(C8H10N)2Cl2] with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The intrinsic fluorescence of BSA could be quenched by Zn(II) complex. The quenching mechanism was suggested as static quenching according to the Stern–Volmer equation. The binding constants Kband the number of binding sites n were calculated. The Zn(II) complex exhibit good binding propensity to bovine serum albumin having relatively high binding constant values. The thermodynamic parameters indicate that the hydrogen bonds and van der Waals forces play a major role in BSA-Zn(II) complex association. The process of binding was spontaneous, in which Gibbs free energy change (ΔG) was negative.

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.

Chemotactic properties, cellular binding and uptake of peptides and peptide derivatives: studies with Tetrahymena thermophila

1992 ◽  
Vol 103 (2) ◽  
pp. 565-570
Author(s):  
V. Leick
Keyword(s):  
Bovine Serum Albumin ◽  
Cell Surface ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tetrahymena Thermophila ◽  
Chemotactic Peptide ◽  
Dansyl Group ◽  
Peptide Derivatives

Receptor-mediated binding of leukocyte chemotactic peptide, N-formylMet-Leu-Phe (fMLP), occurs in the ciliated protozoon Tetrahymena thermophila. In vivo labelling of the cells with N-formylMet-Leu-[3H]Phe ([3H]fMLP) shows that the cells bind the ligand with high affinity (KD = 4 × 10(−9) M to 1 × 10(−8) M). Moreover, Scatchard transformations of the binding data show that there are about 5 × 10(5) binding sites per cell on the cell surface. Two fluorescent derivatives of leukocyte chemotactic peptide, N-dansylMet-Leu-Phe (dansMLP) and N-formylMet-Leu-Phe-(N-dansyl-)Lys (fMLPdanLys) compete for the N-formylMet-Leu-Phe (fMLP) binding sites on the cell surface. Moreover, both derivatives have retained significant chemoattracting potentials. Fluorescence from dansMLP, but not from fMLPdansLys and dansyl-beta-endorphin, is internalized preferentially into small vesicles. The differences may, however, reflect that the fluorescence from the dansyl group is strongly quenched by a hydrophilic microenvironment when using the two latter peptide derivatives. In contrast, the dansyl group from dansMLP must be assumed to be embedded in a hydrophobic microenvironment in the vesicular membrane or membrane protein. Rhodamine-labelled bovine serum albumin, egg albumin and cytochrome c as well as dansylated bovine serum albumin, which are poor chemoattractants, are preferentially seen to be internalized into large vesicles (food vacuoles).

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