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A biochromatographic framework to evaluate the calcium effect on the antihypertensive molecule-human serum albumin
Claire André1, Mireille Thomassin, Catherine Guyon
1Equipe des Sciences Séparatives et Biopharmaceutiques (2SB), Laboratoire de Chimie Analytique, Faculté Médecine Pharmacie, Univ. de Franche-Comte, Place Saint-Jacques, Besançon 25030, Cedex, France.
Abstract:
The Ca(2+) cation effect on the antihypertensive molecule binding on human serum albumin (HSA) was studied by biochromatography. The thermodynamic parameters corresponding to this binding were determined for a wide range of Ca(2+) concentration (x). For the two antihypertensive molecules under study, their binding to HSA can be divided into two Ca(2+) cation concentration regions due to a HSA phase transition. This result was confirmed by an enthalpy-entropy investigation. For a low x value (below x(c)=1.6 mmol l(-1)), the HSA cavity was in an ordered solid-like state leading to an increase in the interactions between the antihypertensive drugs and the HSA cavity and consequently, a solute-HSA affinity increase. For x above x(c), the HSA cavity was in a disordered solid-like state, implying a decrease in the antihypertensive drug-HSA binding.