scholarly journals Relation between Macroscopic Binding Constant and the Anticancer Efficacy of the Bovine Serum Albumin-Quercetin Complex against Drug-Sensitive and Drug-Resistant Cells

2011 ◽  
Vol 7 (1) ◽  
pp. 10-20 ◽  
Author(s):  
Choiprasert
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Drug Resistant ◽  
Anticancer Efficacy ◽  
Resistant Cells

The Study on the Interaction Conditions of Water-Soluble Chitosan with Bovine Serum Albumin

2011 ◽  
Vol 347-353 ◽  
pp. 1281-1286
Author(s):  
Shan Shan Huang ◽  
Feng Zuo Qu ◽  
Tong Kuan Xu ◽  
Li Cui
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Linear Relationship ◽  
Binding Constant ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Water Soluble ◽  
Visible Absorption

The interaction conditions between the water-soluble chitosans(WSC) and bovine serum albumin (BSA) was studied by Ultraviolet-visible absorption and fluorescence spectrometries. It was shown there was a good linear relationship between the absorbency A and the BSA concentration(0~1.5g/L) and WSC concentration (0~1.5 g/L). The fluorescence quenching of WSC to BSA was static quenching. When the temperature is 30°C, its binding constant Ka=5.35×104 L/mol, binding site n=1.05. The influence of WSC on the conformation of BSA was analyzed by sychronous fluorescence spectra and three-dimensional fluorescence spectrum.

The Effect of Bovine Serum Albumin on the Binding Constant and Stoichiometry of Biocompatible Magnetic Fluids

2004 ◽  
Vol 40 (4) ◽  
pp. 3027-3029 ◽  
Author(s):  
P.P. Macaroff ◽  
D.M. Oliveira ◽  
Z.G.M. Lacava ◽  
R.B. Azevedo ◽  
E.C.D. Lima ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Magnetic Fluids

The Investigation of the Interaction between Daidzin and Bovine Serum Albumin by Fluorescence Spectroscopy

2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Hydrogen Bonds ◽  
Fluorescence Quenching ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Apparent Binding Constant

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.

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.

scholarly journals Antibacterial Activity of BSA-Capped Gold Nanoclusters against Methicillin-Resistant Staphylococcus aureus (MRSA) and Vancomycin-Intermediate Staphylococcus aureus (VISA)

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Shu-Hua Kuo ◽  
Chi-Sheng Chien ◽  
Chun-Chi Wang ◽  
Chi-Jen Shih
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Gold Nanoclusters ◽  
Drug Resistant ◽  
Fluorescence Image ◽  
Methicillin Resistant

The emergence of drug-resistant pathogens and the abuse of antibiotics have posed dominant threats to society. In this study, we propose an antibacterial use of bovine serum albumin-capped gold nanoclusters (BSA-AuNCs) to address the issue. BSA-AuNCs have a great antibacterial activity against MRSA and VISA which is proved by time-killing curves (TKC). The possible antibacterial mechanisms of BSA-AuNCs against MRSA and VISA are confirmed by fluorescence image observation.

Microwave synthesis and photophysics of new tetrasulfonated tin(II) macrocycles

2007 ◽  
Vol 11 (02) ◽  
pp. 109-117 ◽  
Author(s):  
Samson Khene ◽  
Abimbola Ogunsipe ◽  
Edith Antunes ◽  
Tebello Nyokong
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Microwave Synthesis ◽  
Binding Constant ◽  
Bovine Serum ◽  
Aqueous Media ◽  
Triton X

This work reports on the microwave synthesis of tetrasulfonated tin phthalocyanine and tetrasulfonated tin α,β,γ-tetrabenzcorrole. The latter was only formed at low ratios (<1:8) of 4-sulfophthalic acid to urea. Both complexes are aggregated in aqueous media, but can be partly or fully disaggregated by the addition of Triton X-100. The α,β,γ-tetrabenzcorrole complex has lower triplet life times and yields, while the binding constant and quenching (of bovine serum albumin) constant are lower for α,β,γ-tetrabenzcorrole compared to tetrasulfonated tin phthalocyanine.

Study on the interaction of bovine serum albumin with acid cyanine 5R and its application in analysis

2006 ◽  
Vol 84 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Fei Lu ◽  
Jing-Hao Pan ◽  
Yun Liu ◽  
Hongfen Zhang ◽  
Yujing Guo ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Peak Potential ◽  
Buffer Solution ◽  
Solution Ph ◽  
Peak Current ◽  
Binding Ratio ◽  
Relative Standard

A supramolecular complex of bovine serum albumin (BSA) with acid cyanine 5R (AC 5R, C.I. acid blue 113, C.I.: 26360) has been shown to form in Tris–HCl buffer solution (pH 7.42) by linear sweep voltammetry (LSV), fluorimetry, and spectrophotometry. The binding ratio and binding constant of BSA with AC 5R have been detected by LSV and fluorimetry. The binding mechanism is also preliminarily discussed. In Tris–HCl buffer solution (pH 7.42), AC 5R can easily be reduced on the mercury electrode, and it has a well-defined LSV peak current (Ip) and peak potential (Ep) at –0.65 V (vs. SCE). In the presence of BSA, the Ipof AC 5R decreases, and the peak potential (Ep) shifts to a more positive potential. The decrease of the second-order derivative of reductive peak current (ΔIp") of AC 5R is proportional to the logarithm of BSA concentration in the range of 1.54 × 10–8mol·L–1– 1.54 × 10–5mol·L–1(r = 0.9931 – 0.9977). The limit of detection of BSA is 9.0 × 10–9mol·L–1. The relative standard deviation is 1.83% (n = 10), and the standard recovery is 97.5%–104.8%. This method can be used to determine BSA concentration on the basis of the interaction of BSA with AC 5R.Key words: bovine serum albumin (BSA), acid cyanine 5R (AC 5R), supramolecule, binding ratio, binding constant, fluorimetry, spectrophotometry, electroanalytical method.

Interaction of a novel platinum drug with bovine serum albumin: FTIR and UV-Vis spectroscopy analysis

2015 ◽  
Vol 39 (7) ◽  
pp. 5676-5685 ◽  
Author(s):  
Filiz Korkmaz ◽  
Deniz Altunoz Erdogan ◽  
Şeniz Özalp-Yaman
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Spectroscopy Analysis ◽  
Platinum Drug ◽  
Hydrophobic Cavity ◽  
Low Concentrations ◽  
Vis Spectroscopy

Platinum-Blue docks at a hydrophobic cavity at low concentrations with a binding constant comparable to that of cisplatin.

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