André Claire, Thomassin Mireille, Guyon Catherine, Truong Tong-Thanh, Guillaume Yves-Claude
Equipe des Sciences Séparatives et Biopharmaceutiques (2SB), Laboratoire de Chimie Analytique, Faculté Médecine Pharmacie, Univ. de Franche-Comte, Place Saint-Jacques, Besançon 25030, Cedex, France.
J Pharm Biomed Anal. 2003 Jun 1;32(2):217-23. doi: 10.1016/s0731-7085(03)00077-3.
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.
通过生物色谱法研究了Ca(2+)阳离子对降压分子与人血清白蛋白（HSA）结合的影响。针对广泛的Ca(2+)浓度（x）测定了与该结合相应的热力学参数。对于所研究的两种降压分子，由于HSA的相变，它们与HSA的结合可分为两个Ca(2+)阳离子浓度区域。焓-熵研究证实了这一结果。对于低x值（低于x(c)=1.6 mmol l(-1)），HSA腔处于有序的固态，导致降压药物与HSA腔之间的相互作用增加，从而溶质-HSA亲和力增加。对于x高于x(c)，HSA腔处于无序的固态，这意味着降压药物与HSA的结合减少。
