scholarly journals The Synthesis of Wavelength-Controlled CdTe/Hydroxyapatite Composites and Their Fluorescence Enhancement by Bovine Serum Albumin

2016 ◽  
Vol 2016 ◽  
pp. 1-10 ◽  
Author(s):  
Li Jin ◽  
Lihua Na ◽  
Xueling Cao ◽  
Fangli Zhong ◽  
Jianpo Zhang
Keyword(s):  
Quantum Dots ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Emission Intensity ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Fluorescence Emission ◽  
Biochemical Processes ◽  
Before And After ◽  
A Site

For the last ten years, quantum dots modified by biological materials have made it possible to study biochemical processes by means of biomedical imaging. This thesis introduced how the fluorescence CdTe quantum dots/hydroxyapatite composites were synthesized and how their structure, morphology, and fluorescence property were characterized by using TEM, XRD, EDS, UV-vis absorption spectra, and fluorescence spectra. The fluorescence spectra indicated the superb photometric characteristics of CdTe/HA composites. We also found that refluxing temperature and time had prominent effects on fluorescence wavelength and intensity of CdTe/HA composites, so the fluorescence emission wavelength of CdTe/HA composites could be controlled. In addition, the effect of BSA on the fluorescence properties of CdTe/HA composites was studied. The fluorescent emission intensity of CdTe/HA composites was enhanced directly with increasing concentrations of BSA; meanwhile, the fluorescence emission intensity of BSA dramatically decreased, which indicated that a Förster nonradiative energy transfer process occurred through the formation of chemical bonds between BSA and CdTe/HA composites. And the two-dimensional correlation (2D COS) was used to analyze the BSA solution before and after the reaction, which indicated that CdTe/HA composites have bound to a site at the surface of the molecule in the first subdomain IA. We also found that there was a linear relationship between the fluorescence intensity enhancement (F/F0) of CdTe/HA composites and the concentration of the bovine serum albumin, which might become a method for quantitative analysis of BSA in a real sample.

scholarly journals Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements

2017 ◽  
Vol 19 (26) ◽  
pp. 17143-17155 ◽  
Author(s):  
Dmitry Molodenskiy ◽  
Evgeny Shirshin ◽  
Tatiana Tikhonova ◽  
Andrey Gruzinov ◽  
Georgy Peters ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Interaction Potential ◽  
Protein Interactions ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
Thermally Induced ◽  
Before And After

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.

Effect of Crystals Size, Surface Area and Pore Size of Hydroxyapatite Microspheres on the Loading Ability of Bovine Serum Albumin

2011 ◽  
Vol 197-198 ◽  
pp. 17-20
Author(s):  
Jun Ming Li ◽  
Ai Juan Wang ◽  
Yu Peng Lv ◽  
Bai Ling Jiang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Specific Surface ◽  
Pore Size ◽  
Surface Area ◽  
Specific Surface Area ◽  
Bovine Serum ◽  
Crystal Size ◽  
Adsorption Ability ◽  
Before And After

Effect of crystals size, surface area, pore size and porosity of hydroxyapatite microspheres on the loading ability of bovine serum albumin was studied in this paper. The surface morphology, specific surface area and porosity of hydroxyapatite microspheres were characterized by scanning electron microscope, specific surface area and pore size analyzer, respectively. The concentration of BSA in aqueous solutions both before and after adsorption was determined by ultraviolet-visible spectrophotometer. The results indicated that the adsorption behavior of bovine serum albumin appeared to obey the Langmuir-type isotherm model. Fast adsorption appeared at the beginning, and then decreased gradually. Hydroxyapatite microspheres calcined at 600°C had the maximum capacity, and those calcined at 800°C showed lower adsorption ability. The loading ability of hydroxyapatite microspheres depended on its crystal size, specific surface area, pore size and porosity, etc.

scholarly journals Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

2013 ◽  
Vol 36 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol-Khalegh Bordbar ◽  
Yadolahe Khodadusdt
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Conformation ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Aggregate Formation ◽  
Cationic Porphyrin ◽  
Porphyrin Complex ◽  
Induced Aggregation

The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

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.

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