کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1548577 997746 2009 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Conformation-activity studies on the interaction of berberine with acetylcholinesterase: Physical chemistry approach
موضوعات مرتبط
مهندسی و علوم پایه مهندسی مواد مواد الکترونیکی، نوری و مغناطیسی
پیش نمایش صفحه اول مقاله
Conformation-activity studies on the interaction of berberine with acetylcholinesterase: Physical chemistry approach
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Progress in Natural Science - Volume 19, Issue 12, 10 December 2009, Pages 1721–1725
نویسندگان
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