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Calorimetric and spectroscopic studies of the interaction between zidovudine and human serum albumin.
Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 2018 Februrary 16
A quantitative analysis of the interaction between zidovudine (AZT) and human serum albumin (HSA) was achieved using Isothermal titration calorimetry (ITC) in combination with fluorescence and 1 H NMR spectroscopy. ITC directly measure the heat during a biomolecular binding event and gave us thermodynamic parameters and the characteristic association constant. By fluorescence quenching, the binding parameters of AZT-HSA interaction was determined and location to binding site I of HSA was confirmed. Via T1 NMR selective relaxation time measurements the drug-protein binding extent was evaluated as dissociation constants Kd and the involvement of azido moiety of zidovudine in molecular complex formation was put in evidence. All three methods indicated a very weak binding interaction. The association constant determined by ITC (3.58×102 M-1 ) is supported by fluorescence quenching data (2.74×102 M-1 ). The thermodynamic signature indicates that at least hydrophobic and electrostatic type interactions played a main role in the binding process.
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