Binding of p-Cresylsulfate and p-Cresol to Human Serum Albumin Studied by Microcalorimetry

被引:36
作者
Berge-Lefranc, David [1 ]
Chaspoul, Florence [1 ]
Calaf, Raymond [2 ]
Charpiot, Philippe [2 ,3 ]
Brunet, Philippe [3 ]
Gallice, Philippe [1 ]
机构
[1] Univ Mediterranee, Fac Pharm,EA 1784, Lab Chim Gen Prevent Ris & Nuisances Technol, Biogenotox & Mutagenese Environm FR3098,ECCOREV, F-13005 Marseille, France
[2] Univ Mediterranee, Fac Pharm, Lab Biochim Fondamentale Mol & Clin, F-13005 Marseille, France
[3] Univ Mediterranee, Fac Pharm, Lab Hematol Immunol, INSERM,U608, F-13005 Marseille, France
关键词
MASS SPECTROMETRIC ANALYSIS; PLASMA-PROTEIN-BINDING; UREMIC TOXINS; CARDIOVASCULAR-DISEASE; EQUILIBRIUM DIALYSIS; ULTRAFILTRATION; BACTERIA; SULFATE; REMOVAL; SOLUTES;
D O I
10.1021/jp9059517
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
p-Cresylsulfate, a metabolite of p-cresol, is reported as prototypic protein-bound Uremic toxin, inefficiently removed by haemodialysis. The binding between p-cresylsulfate or p-cresol and human serum albumin was Studied using rnicrocalorimetry. The results confirm that the two molecules are protein-bound. However. the affinity of p-cresylsulfate and p-cresol toward human serum albumin is moderate at 25 degrees C and becomes relatively weak at physiological temperature, 37 degrees C. The binding principally involves van der Waals type interactions, and the binding sites of the two molecules are the same or very close, The low fraction of bound toxin (13-20%) appears to be insufficient to link strong binding to poor removal of this toxin by hemodialysis.
引用
收藏
页码:1661 / 1665
页数:5
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