Journal
PROGRESS IN NATURAL SCIENCE-MATERIALS INTERNATIONAL
Volume 19, Issue 12, Pages 1721-1725Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.pnsc.2009.07.010
Keywords
Acetylcholinesterase; Berberine; Interaction; Isothermal titration calorimetry; Spectroscopy
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Berberine has been reported as an acetylcholinesterase (AChE) inhibitor. With significantly low cytotoxicity, berberine will be developed for the clinical treatment of Alzheimer disease (AD) with higher efficacy and fewer side effects. This work investigated the structure change events of AChE that occur during the interaction with berberine by isothermal titration calorimetry (ITC), fluorescence titration, and circular dichroism (CD). The results show that the binding of berberine to AChE is mainly driven by a favorable entropy increase with a less weak affinity. Berberine causes a loss in enzymatic activity at a concentration much below the concentration which gradually exposed the tryptophan residues to a more hydrophilic environment and unfolded the protein, which indicates that the inhibition of AChE with berberine includes the main contributions of interaction and minor conformation change of the protein induced by the alkaloid. (C) 2009 National Natural Science Foundation of China and Chinese Academy of Sciences. Published by Elsevier Limited and Science in China Press. All rights reserved.
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