Glycyrrhizin Binding Site on Human Serum Albumin

• Published in: Chem. Pharm. Bull Vol. 40; no. 1; pp. 275 - 278
• Main Authors: ISHIDA, Shiro, KINOSHITA, Masahiro, SAKIYA, Yoko, TAIRA, Zenei, ICHIKAWA, Tsutomu
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 01.01.1992; 公益社団法人日本薬学会; Maruzen
• Subjects: binding site; Binding Sites; Biological and medical sciences; competitive inhibition; deoxycholic acid; General pharmacology; Glycyrrhetinic Acid - analogs & derivatives; Glycyrrhetinic Acid - blood; Glycyrrhizic Acid; glycyrrhizin; human serum albumin; Humans; ibuprofen; Medical sciences; Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions; Pharmacology. Drug treatments; Protein Binding; salicylate; Serum Albumin - metabolism; ultrafiltration technique; warfarin; Human; Proteins; Chemical shift; Biological fixation; Specificity; Investigation method; Albumin; Serum; Binding site; Blood; Bound form
• ISSN: 0009-2363; 1347-5223
• DOI: 10.1248/cpb.40.275

The binding site of glycyrrhizin (GLZ) on human serum albumin was detected through competitive displacement experiments with GLZ and ibuprofen (IBU)(diazepam site), warfarin (WAR), salicylate (SAL)(digitoxin site), or deoxycholic acid (DCA) by means of an ultrafiltration technique. The specific binding of GLZ was subject to competitive inhibition by IBU, WAR, SAL, or DCA (1 or 4mM). The extent of displacement was in the order of : DCA>IBU>WAR>SAL. Conversely, the specific bindings of WAR and DCA and the low-affinity bindings of IBU and SAL were subject to competitive inhibition by GLZ (1 or 4mM). The extent of inhibition by GLZ was in hte order of DCA>IBU>WAR≒SAL. In addition, the low-affinity IBU binding and the specific DCA binding showed mutual competitive inhibition at 4mM, with almost identical displacements. It was concluded that the specific GLZ binding site on human serum albumin may be located mostly within the low-affinity IBU binding site area (probaly the same as the specific DCA binding site area) and partially within the specific WAR binding site area and the low-affinity SAL binding site area.