Reanalysis of the testosterone displacement from its HSA binding site by DHEA using competitive Langmuir isotherm

In a previous manuscript [C. Andre, A. Berthelot, J.F. Robert, M. Thomassin, Y.C. Guillaume, J. Pharm. Bio. Med., in press], the Mg2+ effect on the testosterone displacement equilibrium from its human serum albumin (HSA) binding site by DHEA was investigated using a thermodynamic approach. In this paper, a novel concept based on the competitive Langmuir distribution isotherms was proposed to calculate the association constant of the HSA–hormone binding and to confirm the Mg2+ role on the testosterone displacement equilibrium from its HSA binding site by DHEA. Thus, both the HSA–hormone binding and the displacement equilibrium processes were reanalysed. The results obtained confirmed that:– nd testosterone bound on the same HSA site; isplaced well testosterone to its HSA binding site; ation led a change on both the HSA–hormone binding and the displacement equilibrium at a critical Mg2+ concentration xc around 1 mM.