Albumin, binding properties

Mahmut Dunnus, Hanifi Yaman, Cem Gol, Vefa Ahsen, Tebello Nyokong. (2011). Water-soluble quatemized mercaptopyridine-substituted zinc-phthalocyanines Synthesis, photophysical, photochemical and bovine serum albumin binding properties. Dyes and Pigments 91, 153-163. 

This section will provide an overview on ADME models from our group to illustrate our approach for building predictive models on structurally diverse training sets. Datasets for intestinal human absorption and human serum albumin binding are discussed, while models for other relevant ADME properties have also been obtained. Those models, however, do not stand alone but are used in combination with those models tailored for affinity and selectivity in the frame of multidimensional lead optimization. 

King, T. P. and Spencer, E. M. 1970. Structure studies and organic ligand-binding properties of bovine plasma albumin. J. Biol. Chem. 245, 6134-6148. 

Kragh-Hansen U (1990) Structure and ligand binding properties of human serum albumin. Dan Med Bull 37(l) 57-84... 

W. A. Tao and R. K. Gilpin, Liquid chromatographic studies of the effect of phosphate on the binding properties of sihca-immobilized bovine serum albumin, J. Chromatogr. Sci. 39 (2001), 205. 

Etacrynic acid interacts with human serum albumin and modifies its binding properties (45). Since it binds to two binding sites on albumin, the benzodiazepine binding site and the warfarin binding site, it can displace drugs that bind at those sites (46). It competitively displaced 7-hydroxymethotrexate from its binding proteins in vitro (47). The clinical significance of this effect is not known. 

Often utilized as a substitute for a typical protein, albumin needs no introduction to the protein chemist. Because of its availability, low cost, stability, and unusual ligand-binding properties, serum albumin has been one of the most extensively studied and applied proteins in biochemistry. However, as a protein, albumin is far from typical, and the widespread interest in and application of albumin have not been balanced by an understanding of its molecular structure. Indeed, for more than 30 years structural information was surmised based solely on techniques such as hydrodynamics, low-angle X-ray scattering, and predictive methods. 

The function of most albumin isoforms is normal, although some have abnormal binding affinities for thyroxine (T4). Binding may be increased, as in familial dysalbu-minemic hyperthyroxinemia, or decreased. Individuals with famihal dysalbuminemic hyperthyroxinemia are euthyroid but have elevated serum T4 and free T4 index the variant albumin comigrates with Alb A. Two glycosylated variants. Alb RedhiU and Alb Casebrook, have altered fatty acid binding properties. 

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