Differential mode of interaction of ThioflavinT with native β structural motif in human α 1-acid glycoprotein and cross beta sheet of its amyloid: Biophysical and molecular docking approach
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- 作者：Mohammad Rehan Ajmala ; Saima Nusrata ; Parvez Alama ; Nida Zaidia ; Gamal Badrb ; Mohamed H. Mahmoudc ; d ; Ravi Kant Rajpoote ; Rizwan Hasan Khana ; rizwanhkhan1@gmail.com" class="auth_mail" title="E-mail the corresponding author ; rizwanhkhan1@yahoo.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Alpha-1 acid glycoprotein ; Fluorescence spectroscopy ; Isothermal titration calorimetry ; Molecular docking ; Circular dichroism
- 刊名：Journal of Molecular Structure
- 出版年：2016
- 出版时间：5 August 2016
- 年：2016
- 卷：1117
- 期：Complete
- 页码：208-217
- 全文大小：2104 K
文摘
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Human α1-acid glycoprotein is major acute phase glycoprotein in human plasma and interacts with Thioflavin T.
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Fluorescence data suggested binding constant in order of 105.
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Isothermal titration calorimetry suggested endothermic nature of the binding reaction.
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CD and DLS suggested conformational alterations in the protein due to binding process.
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Molecular docking revealed the involvement of central beta barrel structure of protein in binding process.