Analysis of the progesterone displacement of its human serum albumin binding site by beta-estradiol using biochromatographic approaches: effect of two salt modifiers.
The mechanisms of (i) the binding of two sex-hormones (i.e. progesterone and beta-estradiol) to human serum albumin (HSA) and (ii) the progesterone displacement of its HSA binding cavity by beta-estradiol were studied by biochromatography using three different methods. In the first time, zonal elution method was used to prove the direct competition effect between the two sex-hormone. In the second time, the competition effect between beta-estradiol and progesterone to bound on the same HSA site was analysed by the competitive bi-Langmuir approach. Finally, the thermodynamic data of these two binding processes were studied. The Gibbs free energy value (Delta(approximately)G degrees) of the displacement equilibrium was negative demonstrating that beta-estradiol displaced progesterone of its HSA binding cavity. Moreover, the effect of two chloride modifiers (i.e. Na(+), Mg(2+)) on these two binding processes were analysed. Results showed that in the salt biological concentration ranges, the Mg(2+) cation enhanced strongly the bioavailable progesterone, whereas the Na(+) cation interacted slowly on the progesterone displacement of its HSA binding site by beta-estradiol. This study showed that it must be useful to carry out more in vivo test on the magnesium supplementation effect for women who suffer from estrogen dominance syndrome.
André
C
C
Equipe des Sciences Séparatives et Biopharmaceutiques (2SB), Laboratoire de Chimie Analytique, Place Saint-Jacques, 25030 Besançon Cedex, France.
Jacquot
Y
Y
Truong
T T
TT
Thomassin
M
M
Robert
J F
JF
Guillaume
Y C
YC
D001667:Binding, Competitive; D004958:Estradiol / Q000378:metabolism*; D006801:Humans; D011374:Progesterone / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D013816:Thermodynamics
D012709:Serum Albumin; D011374:Progesterone; D004958:Estradiol