Complex interaction of caffeic acid with bovine serum albumin: calorimetric, spectroscopic and molecular docking evidence

2017 ◽  
Vol 41 (24) ◽  
pp. 15003-15015 ◽  
Author(s):  
Aurica Precupas ◽  
Romica Sandu ◽  
Anca Ruxandra Leonties ◽  
Dan-Florin Anghel ◽  
Vlad Tudor Popa

Binding of caffeic acid at low concentrations to bovine serum albumin enhances the thermal stability of the protein.

2020 ◽  
Vol 22 (42) ◽  
pp. 24410-24422
Author(s):  
Kavya Bhakuni ◽  
Niketa Yadav ◽  
Pannuru Venkatesu

This study unravels the effect of a novel solvent medium designed by amalgamation of macromolecular crowders and deep eutectic solvents (DESs) on bovine serum albumin (BSA).


2015 ◽  
Vol 17 (2) ◽  
pp. 1114-1133 ◽  
Author(s):  
Bhupender S. Gupta ◽  
Mohamed Taha ◽  
Ming-Jer Lee

In this study, we have analyzed the influence of four biological buffers on the thermal stability of bovine serum albumin (BSA) using dynamic light scattering (DLS).


2011 ◽  
Vol 15 (04) ◽  
pp. 223-229 ◽  
Author(s):  
Natalia Lebedeva ◽  
Tatyana Popova ◽  
Malgorzata Kozbial ◽  
Malgorzata Wszelaka-Rylik ◽  
Yuri Gubarev ◽  
...  

Interaction between bovine serum albumin (BSA) and tetraantraquinoporphyrazines (TAP) and tetrasulphophthalocyanine (Pc) aluminum hydroxide was studied by means of electron absorption spectroscopy, IR spectroscopy, fluorescence spectroscopy and differential scanning calorimetry. It was found that the complex formation of BSA with the TAPs results in increase of thermal stability of the protein while Pc does not have remarkable influence on the protein thermal denaturation.


2010 ◽  
Vol 39 (1) ◽  
pp. 38-39 ◽  
Author(s):  
Roberto Lavecchia ◽  
Antonio Zuorro

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