A novel binding site for bile acids on human serum albumin |
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| Institution: | 1. Department of Chemistry, Panjab University, Chandigarh 160014 India;2. School of Science, Faculty of Science, Engineering and Technology, Swinburne University of Technology, Hawthorn, Victoria 3122 Australia;1. National Centre of Excellence in Analytical Chemistry, University of Sindh, Jamshoro 76080, Pakistan;2. Universidade Estadual Paulista (UNESP), Department of Analytical Chemistry, Institute of Chemistry, Rua Professor Francisco Degni, 55, Quitandinha, 14.800-060 Araraquara, Brazil;3. Neuro Diagnostic Centre, Liaquat University of Medical & Health Sciences, Jamshoro, Pakistan;1. Center for Integrated Protein Science, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany;2. Department of Informatics, Ludwig-Maximilians-Universität München, Amalienstr. 17, 80333 München, Germany;3. Physics Department, Technische Universität München, James-Franck-Strasse 1, 85747 Garching, Germany |
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| Abstract: | Binding sites of bile acids on human serum albumin were studied using various probes: dansylsarcosine (site I probe), 7-anilinocoumarin-4-acetic acid (ACAA, site II probe), 5-dimethylaminonaphthelene-1-sulfonamide (DNSA, site III probe), cis-parinaric acid (probe for fatty acid binding site) and bilirubin. Bile acids competitively inhibited the binding of dansylsarcosine to human serum album whereas bile acids enhanced the binding of ACAA, DNSA, cis-parinaric acid and bilirubin. Considering the concentrations of bile acids required to inhibit the binding of dansylsarcosine to human serum albumin, the secondary binding site of bile acids may correspond to site I. Dissociation constants (Kd) of the primary binding sites of lithocholic and chenodeoxycholic acid to human serum albumin were approximately 0.2 and 4 μM, respectively, which was measured by equilibrium dialysis at 37° C. All the bile acids and their sulfates and glucuronides inhibited the binding of chenodeoxycholic acid to human serum albumin. Lithocholic and chenodeoxycholic acid and their sulfates and glucuronides exhibited more inhibition than cholic acid and its conjugates. In conclusion, bile acids may bind to a novel binding site on human serum albumin. |
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