Nanoparticle–Protein Interactions: A Thermodynamic and Kinetic Study of the Adsorption of Bovine Serum Albumin to Gold Nanoparticle Surfaces

Langmuir ◽  
2013 ◽  
Vol 29 (48) ◽  
pp. 14984-14996 ◽  
Author(s):  
Stefano P. Boulos ◽  
Tyler A. Davis ◽  
Jie An Yang ◽  
Samuel E. Lohse ◽  
Alaaldin M. Alkilany ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Kinetic Study ◽  
Gold Nanoparticle ◽  
Protein Interactions ◽  
Bovine Serum

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.

Kinetic Study on the Interaction Between 5-Sulfosalicyclic Acid and Bovine Serum Albumin with a Wireless Magnetoelastic Biosensor

2009 ◽  
Vol 7 (2) ◽  
pp. 148-152
Author(s):  
Xianjuan Gao ◽  
Yujun Zhang ◽  
Chuntao Zhao ◽  
Xiaolei Sheng ◽  
Ruiyan Zhen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Kinetic Study ◽  
Bovine Serum

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.

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