Allosteric modulation of drug binding to human serum albumin

被引:151
作者
Ascenzi, P
Bocedi, A
Notari, S
Fanali, G
Fesce, R
Fasano, M
机构
[1] IRCCS, Ist Nazl Malattie Infett, I-00149 Rome, Italy
[2] Univ Insubria, Dipartimento Biol Strutt & Funz, I-21052 Busto Arsizio, VA, Italy
[3] Univ Insubria, Ctr Neurosci, I-21052 Busto Arsizio, VA, Italy
关键词
human serurn albumin; drug binding; structure; allostery; structure-activity relationship; biomedical aspects;
D O I
10.2174/138955706776361448
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Human serum albumin (HSA), the most prominent protein in plasma, is best known for its extraordinary ligand binding capacity. The three homologous domains of HSA (labeled 1, 11, and 111), each in turn composed of two subdomains (named A and B), give rise to the three-dimensional structure of HSA. This flexible structural organization allows the protein structure to adapt to a variety of ligands. As conformational adaptability of HSA extends well beyond the immediate vicinity of the binding site(s), cooperativity and allosteric modulation arise among binding sites; this makes HSA similar to a multimeric protein. Although kinetic and thermodynamic parameters for ligand binding to HSA calculated by quantitative structure-activity relationship models are in excellent agreement with those obtained in vitro, cooperative and allosteric equilibria between different binding sites and competition between drugs or between drugs and endogenous ligands make difficult the interpretation of HSA binding properties in vivo. Binding of exogenous and endogenous ligands to HSA appears to be relevant in drug therapy and management. Here, the allosteric modulation of drug binding to HSA is briefly reviewed.
引用
收藏
页码:483 / 489
页数:7
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