In-depth insight into the methods of plasma protein-drug interaction studies: Comparison of capillary electrophoresis-frontal analysis, isothermal titration calorimetry, circular dichroism and equilibrium dialysis

2017 ◽  
Vol 39 (4) ◽  
pp. 581-589 ◽  
Author(s):  
Hana Nevídalová ◽  
Lenka Michalcová ◽  
Zdeněk Glatz
2001 ◽  
Vol 204 (5) ◽  
pp. 1033-1038 ◽  
Author(s):  
M. Menze ◽  
N. Hellmann ◽  
H. Decker ◽  
M. Grieshaber

Haemocyanin serves as an oxygen carrier in the haemolymph of decapod crustaceans. The oxygen-binding behaviour of the pigment is modulated by the two major anaerobic metabolites, l-lactate and urate. The binding of these two metabolites to haemocyanin has been investigated mainly indirectly by following the effector-induced changes in the oxygen-binding properties of the respiratory pigment. Only a few direct investigations of effector binding, employing ultracentrifugation techniques and equilibrium dialysis, have been carried out. No evidence for cooperative binding for either effector was detected using these methods. However, isothermal titration calorimetry (ITC) offers a useful tool to gain additional insight into the binding of effectors to these highly allosterically regulated macromolecules. By applying the ITC method to the fully oxygenated dodecameric haemocyanin of the lobster Homarus vulgaris, cooperativity in binding has been found for the urate analogue caffeine but not for urate itself: using urate and the urate analogue caffeine as ligands, two conformations of the oxygenated pigment were detected.


2016 ◽  
Vol 46 (8) ◽  
pp. 1491-1497
Author(s):  
Monique Barreto Santos ◽  
Bernardo de Sá Costa ◽  
Edwin Elard Garcia Rojas

ABSTRACT: The interactions between biological macromolecules have been important for biotechnology, but further understanding is needed to maximize the utility of these interactions. Calorimetric techniques provide information regarding these interactions through the thermal energy that is produced or consumed during interactions. Notable techniques include differential scanning calorimetry, which generates a thermodynamic profile from temperature scanning, and isothermal titration calorimetry that provide the thermodynamic parameters directly related to the interaction. This review described how calorimetric techniques can be used to study interactions between proteins and polysaccharides, and provided valuable insight into the thermodynamics of their interaction.


2009 ◽  
Vol 10 (3) ◽  
pp. 271-278 ◽  
Author(s):  
Walter de Azevedo Jr. ◽  
Rafael Caceres ◽  
Ivani Pauli ◽  
Luis Fernando Timmers ◽  
Guy Barcellos ◽  
...  

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