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Updated: Mar 1, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Interaction of triterpenoids with human serum albumin: A review
Rola Abboud1, Catherine Charcosset2, Hélène Greige-Gerges3
1Bioactive Molecules Research Laboratory, Faculty of Sciences, Lebanese University, Lebanon; Laboratoire d'Automatique et de Génie des Procédés (LAGEP), UMR-CNRS 5007, Université Claude Bernard Lyon 1, CPE Lyon, Bat 308G, 43 Boulevard du 11 Novembre 1918, F-69622 Villeurbanne Cedex, France.
Abstract:
Triterpenoids are a large group of natural and synthetic products. This review deals with the current state of knowledge on their interaction with serum albumin. The binding of drugs to albumin may control their distribution in tissues. In literature, different techniques were used to investigate the albumin-triterpenoid interaction and include fluorescence spectroscopy, Fourier transform infrared spectroscopy, circular dichroism, calorimetric techniques and molecular modeling. Changes in fluorescence intensity of albumin were observed upon triterpenoid-albumin complex formation. Thermodynamic analyses proved that hydrophobic interactions and hydrogen bonds were the mainly binding forces in triterpenoid-albumin systems. Molecular docking and site marker competitive experimental results revealed that triterpenoids bound to Sudlow's site I of albumin. Furthermore, Fourier transform infrared spectroscopy and circular dichroism spectra analysis indicated that the native conformation of the protein is affected upon binding to triterpenoids.
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