Ligand Binding by Albumin
1995; Elsevier BV; Linguagem: Inglês
10.1016/b978-012552110-9/50005-2
Autores Tópico(s)Drug Transport and Resistance Mechanisms
ResumoAlbumin is best known for its ability to bind smaller molecules of many types. The willingness to take on a varied cargo causes albumin to be likened to a sponge or to a "tramp steamer" of the circulation. The flexibility of the albumin structure adapts it readily to ligands, and its three-domain design provides a variety of sites. The chapter only presents the highlights and conclusions of ligand binding by albumin as literature from protein chemists, cell biologists, nutritionists, pharmacologists, and clinicians still continues to grow. Albumin interacts with a broad spectrum of compounds. Most strongly bound are hydrophobic organic anions of medium size, 100 to 600 Da–long-chain fatty acids, hematin, and bilirubin. Smaller and less hydrophobic compounds such as tryptophan and ascorbic acid are held less strongly, but their binding can still be highly specific. Affinity for the L chiral form of tryptophan exceeds that for the D form by 100-folds.
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