Human serum albumin binding site

Artali, R., Bombieri, G Calabi, L. and Del Pra, A. (2005) A molecular dynamics study of human serum albumin binding sites. IL Farmaco, 60,485-495. 

Sulfaphenazole (684) and sulfazamet (685) are both examples of relatively short acting sulfonamides (B-80MI40406) and their antibacterial activity has been tested against Escherichia coli, the former being more effective than the latter. Sulfaphenazole also displaces sulfonyl ureas from protein binding sites on human serum albumin and consequently increases the concentration of the free (active) drug and produces a more intense reaction that may result in hypoglycemia. 

Soltes, L., Sebille, B. (1997). Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods an attempt to localize the d- and L-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments. Chirality 9, 373-379. 

Curry, S., Mandelkow, H., Brick, P. and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural Biology 5, 827-835. 

Among the series of dyes, in which the effect of binding to human serum albumin (HSA) was studied [41], the dye 8 (Fig. 10) exhibited J-aggregate absorption and fluorescence bands, while these bands were not observed for the free dye. This led to the conclusion about the J-aggregation of the dye 8 in the HSA binding site. 

Y. Ozeki, Y. Kurono, T. Yotosuyanagi, K. Ikeda, Effects of Drug Binding on the Esterase Activity of Human Serum Albumin Inhibition Modes and Binding Sites of Anionic Drugs , Chem. Pharm. Bull. 1980, 28, 535-540. 

Twine, S., East, M., and Curry, S. Crystal structure analysis of warfarin binding to human serum albumin. Anatomy of dmg site I. /. Biol. Chem. 

Benkestock, K., Edlund, P. O., Roeraade, J. Electrospray ionization mass spectrometry as a tool for determination of drug binding sites to human serum albumin by noncovalent interaction. Rapid Commun Mass Spectrom 2005, 19, 1637-1643. 

Scatchard et al found that thiocyanate binding to human serum albumin gave 10 sites with a 1-2 mM dissociation constant, and another 30 with a dissociation constant that was nearly 40 mM. 

Most frequently, binding protein is added to the incubation mixtures as either serum or purified serum albumin. With human serum albumin, at equilibrium, the acceptor substrate will largely be protein-bound, when the bilirubin albumin molecular ratio is smaller than one (the dissociation constant of the first binding site of purified human serum albumin is approximately 7 X 10 M with 2 X 10 M for two additional binding sites) (J2). The first binding site of albumin, measured with rat serum, has a dissociation constant of about 5 X 10" M (M8). The unbound fraction will normally not exceed the very low solubility of the pigment. Addition of albumin to an alkaline solution of bilirubin, or its addition immediately after neutralization, prevents colloid formation, if the bilirubin albumin molecular ratio is smaller than one (B25). However, colloidal bilirubin, once formed, cannot be redissolved by the addition of albumin (B26). 

Brodersen, R., Funding, L., Pedersen, A. O., and Roigaai-d-Petemen, H., Binding of bilirubin to low-affinity sites of human serum albumin in vitro followed by cocrystallization. Scand. J. Clin. Lab. Invest. 29, 343-346 (1972). 

Figure 5 Covalent coupling of cyclic peptide moieties to human serum albumin (HSA). The depicted cyclic peptide, C SRNLIDC, in which C denotes the cyclizing cysteine residues, mimics the receptor binding site of PDGF-BB. First, a sulfhydryl group is introduced to the cyclic peptide by a reaction with succinimide-acetyl thioacetate (SATA). The primary amino groups of lysine in HSA are derivitized with maleimide-hexoyl-At-hydroxysuccinimide ester (MHS). Subsequently, the cyclic peptide is coupled to HSA. In this latter reaction, hydroxyl amine is used to remove the protecting acetate group from the sulfhydryl group of the cyclic peptide.

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