Interaction of some cardiovascular drugs with bovine serum albumin at physiological conditions using glassy carbon electrode: A new approach

2016 ◽  
Vol 65 ◽  
pp. 97-108 ◽  
Author(s):  
Hadi Afsharan ◽  
Mohammad Hasanzadeh ◽  
Nasrin Shadjou ◽  
Abolghasem Jouyban
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Glassy Carbon Electrode ◽  
Glassy Carbon ◽  
Bovine Serum ◽  
Cardiovascular Drugs ◽  
Carbon Electrode ◽  
New Approach ◽  
Physiological Conditions

Voltammetric behavior of Mammeisin (MA) at a glassy carbon electrode and its interaction with Bovine Serum Albumin (BSA)

2018 ◽  
Vol 119 ◽  
pp. 20-25 ◽  
Author(s):  
Jules-Blaise Mabou Leuna ◽  
Sergeot Kungo Sop ◽  
Suzanne Makota ◽  
Evangeline Njanja ◽  
Thiery Christophe Ebelle ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Glassy Carbon Electrode ◽  
Glassy Carbon ◽  
Bovine Serum ◽  
Carbon Electrode ◽  
Voltammetric Behavior

Enantioselective discrimination of l-/d-phenylalanine by bovine serum albumin and gold nanoparticles modified glassy carbon electrode

2015 ◽  
Vol 7 (7) ◽  
pp. 3022-3027 ◽  
Author(s):  
Bingdi Liu ◽  
Xin Zhang ◽  
Yaping Ding ◽  
Liqiang Luo ◽  
Fenfen Zhang
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Gold Nanoparticle ◽  
Glassy Carbon ◽  
Bovine Serum ◽  
Carbon Electrodes ◽  
Carbon Electrode ◽  
Modified Glassy Carbon Electrode ◽  
Glassy Carbon Electrodes

A new chiral biosensor able to discriminate and detect phenylalanine (Phe) enantiomers was fabricated by immobilizing bovine serum albumin (BSA) on gold-nanoparticle-modified glassy carbon electrodes.

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

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