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18β-Glycyrrhetinic acid interaction with bovine serum albumin

Paper ID Volume ID Publish Year Pages File Format Full-Text
28912 44104 2007 6 PDF Available
Title
18β-Glycyrrhetinic acid interaction with bovine serum albumin
Abstract

The interaction of 18β-glycyrrhetinic acid (GA): The metabolite of glycyrrhizic acid which is the main active component of a commonly used traditional Chinese medicine (TCM) Glycyrrhiza Uralensis Fisch with bovine serum albumin (BSA) has been investigated. Fluorescence emission spectra of serum albumin in the presence of GA, recorded at the excitation wavelength 280 nm, clearly show that GA act as quencher and have different quenching mechanism at a pH below or above the isoelectric point (pI). The binding sites number n and apparent binding constant K were measured. The thermodynamic parameters ΔH°, ΔG°, ΔS° at different temperatures were calculated. The effects of some common metal ions on binding are considered. Synchronous fluorescence and UV–vis spectra were used to study protein conformation. Energy transfer between GA and HSA was calculated by Förster's theory and the binding site was suggested to be site II. The binding of monoammonium glycyrrhizinate (GL) to BSA is also compared.

Keywords
18β-Glycyrrhetinic acid; Serum albumin–drug interactions; Fluorescence quenching; Bovine serum albumin; Binding sites
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 185, Issues 2–3, 25 January 2007, Pages 271–276
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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