scholarly journals Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

2017 ◽  
Vol 12 (2) ◽  
pp. 02D404 ◽  
Author(s):  
Brittany E. Givens ◽  
Nina D. Diklich ◽  
Jennifer Fiegel ◽  
Vicki H. Grassian
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Silicon Dioxide ◽  
Protein Interactions ◽  
Bovine Serum ◽  
Silicon Dioxide Nanoparticles

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.

scholarly journals The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small Angle X-Ray Scattering Study

2010 ◽  
Vol 98 (3) ◽  
pp. 630a ◽  
Author(s):  
Leandro R.S. Barbosa ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Sigrid Bernstorff ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Small Angle ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study

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 Adsorption and thermal properties of the bovine serum albumin–silicon dioxide system

2014 ◽  
Vol 120 (2) ◽  
pp. 1355-1364 ◽  
Author(s):  
Małgorzata Wiśniewska ◽  
Katarzyna Szewczuk-Karpisz ◽  
Dariusz Sternik
Keyword(s):  
Thermal Properties ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Silicon Dioxide ◽  
Bovine Serum

Evaluation of a Sound Velocity Analyzer for Estimating Maximum Internal Temperature to Which Meat Products Have Been Heat Processed

1990 ◽  
Vol 53 (8) ◽  
pp. 680-684 ◽  
Author(s):  
W. E. TOWNSEND ◽  
C. E. DAVIS ◽  
R. L. WILSON
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Silicon Dioxide ◽  
Sound Velocity ◽  
Bovine Serum ◽  
Meat Products ◽  
Distilled Water ◽  
Objective Method ◽  
Point Temperature ◽  
End Point Temperature

The sound velocity (SV) values of a variety of solutions (distilled water, saline, silicon dioxide, bovine serum albumin, coagulated beef protein) were determined as the temperature of the solution was increased from 10 or 20° to 71°C. Few differences were found in the SV values for the various types of distilled water; however, there was an increase in SV values as the concentration of saline increased. Level of silicon dioxide or bovine serum albumin had no significant effect on SV values; however, there was an increase in SV values as percentage of precoagulated beef protein solids in solution increased. The sound velocity analyzer used in this study was found not to be sensitive enough to detect the onset of coagulation of saline soluble proteins and, therefore, would not lend itself as an objective method which could be related to end-point temperature of meat products.

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