scholarly journals Determination of the Binding Parameters between Proteins and Luminol by Chemiluminescence Using Flow Injection Technique

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
Jie Guo ◽  
Donghua Chen ◽  
Zhenghua Song
Keyword(s):  
Bovine Serum Albumin ◽  
Flow Injection ◽  
Binding Sites ◽  
Bovine Serum ◽  
Binding Constants ◽  
Injection Technique ◽  
Binding Parameters ◽  
Hydrophobic Force ◽  
Number Of Binding Sites

The interaction behavior of bovine serum albumin (BSA), lysozyme (LYS), myoglobin (MB), and catalase (CAT) with luminol, respectively, was first studied by chemiluminescence (CL) using flow injection (FI) technique based on the fact that the studied proteins can enhance the CL intensity of luminol. A FI-CL model of protein-luminol interaction, lg[(I0−I)/I]=1/nlg[P]+1/nlgKa+2lgn, was constructed, and the interaction parameters of BSA, LYS, MB, and CAT with luminol were determined accordingly. The binding constants Ka are in the descending order of CAT > MB > LYS > BSA at the level of 105 to 107 L mol−1, and the number of binding sites n of luminol to BSA or LYS is around 2 and to MB or CAT is around 1. The results of thermodynamic parameters (ΔH, ΔS, and ΔG) showed that the binding processes of luminol to the four proteins are spontaneous mainly through the hydrophobic force.

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.

Determination of tannic acid after precipitation with bovine serum albumin by visible light scattering in a flow injection system

2010 ◽  
Vol 169 (1-2) ◽  
pp. 117-122 ◽  
Author(s):  
Tzong-Jih Cheng ◽  
Hsien-Yi Hsiao ◽  
Chien-Yu Chung ◽  
Po-Chung Chen ◽  
Richie L. C. Chen
Keyword(s):  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Visible Light ◽  
Tannic Acid ◽  
Flow Injection ◽  
Bovine Serum ◽  
Injection System ◽  
Flow Injection System

scholarly journals Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Xin Zhang ◽  
Jianhong Bian ◽  
Wenjie Zhai ◽  
Jing Dong ◽  
Huihui Liang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Separation ◽  
Anionic Surfactants ◽  
Binding Constants ◽  
Number Of Binding Sites ◽  
Hydrophobic Nature ◽  
Thermodynamic Relationship

The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3′-(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with KA(SNPS) = 8.71×104 M−1 and KA(SNDPS) = 7.08 × 104 M−1, respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.

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 Molecular Modeling and Spectroscopic Studies on the Interaction of Transresveratrol with Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Xiaoli Liu ◽  
Yonghui Shang ◽  
Xudong Ren ◽  
Hua Li
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Binding Sites ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Binding Constants ◽  
Binding Mode ◽  
Spectroscopic Studies

The interaction of transresveratrol (TRES) with bovine serum albumin (BSA) has been investigated by ultraviolet-visible, fluorescence, Fourier transform infrared spectroscopic methods and molecular modeling techniques. The fluorescence results show that the intrinsic fluorescence of BSA is quenched by TRES through a static quenching procedure. The binding constants of TRES with BSA at 292, 297 and 302 K are calculated as10.22×104,8.71×104, and7.59×104 L mol−1, respectively, and corresponding numbers of binding sites are approximately equal to unity. The thermodynamic parameters ΔHand ΔSare estimated to be −21.82 kJ mol−1and +21.15 J mol−1 K−1, which indicates that the interaction of TRES with BSA is driven mainly by hydrophobic forces and there are also hydrogen bonds and electrostatic interactions. The competitive experiments suggest that the binding site of TRES to BSA is probably located on site II. The results of infrared spectra show that the binding of TRES with BSA leads to conformational changes of BSA, and the binding stabilizes theα-helix andβ-sheet at the cost of a corresponding loss in theβ-turn structure of BSA. The results of molecular modeling calculation clarify the binding mode and the binding sites which are in good accordance with the experiment results.

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.

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