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Unraveling the energetics and mode of the recognition of antibiotics tetracycline and rolitetracycline by bovine serum albumin.


Chem Biol Drug Des. 2012 Jul 31;


Authors: Choudhary S, Kishore N


Abstract

An understanding of the detailed energetics and mechanism of the binding of drugs with target proteins is essential for devising guidelines to synthesize new drugs. Binding of the antibiotic drugs tetracycline (TC) and rolitetracycline (RTC) with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calroimetry (DSC), steady state and time resolved fluorescence, and circular dichroism spectroscopies. Both TC and RTC bind to BSA in a sequential manner with first binding being the major binding event with an association constant of the order of 10(4) for TC and 10(3) for RTC, respectively Ionic strength dependence and binding in the presence of tetrabutylammonium bromide and sucrose indicate involvement of a mix of hydrophobic, ionic and hydrogen bonding interactions. The ITC results for the binding of these drugs to BSA in presence of warfarin and in the presence of each other indicate that both these drugs share binding site-2 on BSA. The DSC results provide quantitative information on the effect of drugs on the stability of BSA. A comparison of ITC and fluorescence results demonstrates that the former technique has been able to explain the sequential binding events which can be missed by the fluorescence measurements. © 2012 John Wiley & Sons A/S.

PMID: 22846623 [PubMed - as supplied by publisher]