scholarly journals Investigation of the effects of temperature and ions on the interaction between ECG and BSA by the fluorescence quenching method

2011 ◽  
Vol 63 (2) ◽  
pp. 325-331 ◽  
Author(s):  
Jinyao Zhao ◽  
Xinyu Jiang ◽  
Xin Liu ◽  
Fenglian Ren
Keyword(s):  
Bovine Serum Albumin ◽  
Binding Sites ◽  
Binding Constants ◽  
Epicatechin Gallate ◽  
Number Of Binding Sites ◽  
Fluorescence Quenching Method ◽  
Effects Of Temperature ◽  
Quenching Method ◽  
The Stability ◽  
Increasing Temperature

The effects of temperature and common ions on binding (-)-epicatechin gallate (ECG) to bovine serum albumin (BSA) are investigated. The binding constants (Ka) between ECG and BSA are 1.20 ? 106 (17?C), 1.38 ? 106 (27?C), and 5.69 x 106 L mol-1 (37?C), and the number of binding sites (n) were 1.14, 1.15, and 1.26, respectively. These results showed that the increasing temperature improves the stability of the ECG-BSA system, which results in a higher binding constant and the number of binding sites of the ECG-BSA system. The presence of Co2+ and Zn2+ ions decreased the binding constants (Ka) and the number of binding sites (n) of ECG-BSA complex. However, the presence of Cu2+ and Ni2+ increased the affinity of ECG for BSA largely. The positive ?H and positive ?S indicated that hydrophobic forces might play a major role in the binding between ECG and BSA.

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.

Thermal Stability of Moniliformin at Varying Temperature, pH, and Time in an Aqueous Environment†

2000 ◽  
Vol 63 (11) ◽  
pp. 1598-1601 ◽  
Author(s):  
GRACIELA PINEDA-VALDES ◽  
LLOYD B. BULLERMAN
Keyword(s):  
Animal Species ◽  
Keshan Disease ◽  
Aqueous Environment ◽  
Buffer Solutions ◽  
Processing Times ◽  
Effects Of Temperature ◽  
The Stability ◽  
Increasing Temperature ◽  
Major Reduction ◽  
Thermal Stability Of

Moniliformin (MON) is a widely occurring mycotoxin, produced mainly by Fusarium proliferatum and Fusarium subglutinans in corn, that has been shown to be acutely toxic for various animal species and is a suspected cause of Keshan disease in China. The effects of temperature (100, 125, and 150°C) and pH (4, 7, and 9) on the stability of MON were determined in aqueous buffer solutions at processing times ranging from 10 to 60 min. The percentage of MON reduction was positively related to increasing temperature and pH. MON was most stable at pH 4. After 60 min at pH 4 and 150°C, MON was reduced by only 5%. Heating at pH 10 caused major reduction of MON. After 60 min at pH 10 and 100, 125, and 150°C, MON was reduced by 56, 72, and 83%, respectively. One trial done at 175°C and pH 10 showed that less than 1% MON remained after 60 min of processing.

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 Interaction Between α-Glucosidase Inhibitor with Common Blood Proteins: A Thermodynamic and Spectroscopic Studies

2020 ◽  
Vol 32 (7) ◽  
pp. 1756-1762
Author(s):  
K.M. Sachin ◽  
Sameer A. Karpe ◽  
Man Singh ◽  
Ajaya Bhattarai
Keyword(s):  
Circular Dichroism ◽  
Serum Albumin ◽  
Binding Sites ◽  
Binding Constants ◽  
Spectroscopic Studies ◽  
Blood Proteins ◽  
Glucosidase Inhibitors ◽  
Number Of Binding Sites ◽  
Treatment Of Diabetes ◽  
Circular Dichroïsm

The interaction of an α-glucosidase inhibitors class of drug acarbose with globular proteins like bovine serum albumin (BSA), human serum albumin (HSA) and haemoglobin studied by fluorescence, circular dichroism (CD) spectroscopic methods. Acarbose is used for the treatment of diabetes mellitus type 2 and in some countries, prediabetes. The quenching constant (kq) values were calculated by using fluorescence data, higher with haemoglobin (at λext = 405 nm). It indicates the quenching process for the acarbose-haemoglobin interaction. Thus, the binding constants (kb), infers that the electrostatic, hydrogen bonding, and intermolecular interactions play an important role in the proteins, and drug interaction. The number of binding sites (n), between BSA, HSA and haemoglobin with acarbose was estimated by fluorescence data, the highest binding sites (15.55) of acarbose-haemoglobin at (λext = 405nm) indicates that the strong interaction or high quenching interaction. The interactions between BSA, HSA and haemoglobin with acarbose were confirmed by spectroscopic analysis and thermodynamic determination. The circular dichroism (CD) spectra implied the significant change in the conformation of BSA, HSA and haemoglobin upon binding with acarbose.

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