Article
Insight into the interaction mechanism of thioflavin-t with an amyloid beta (1-42) by the docking method
- Department of Natural Sciences Teacher Education, Dong Thap University, Dong Thap, Vietnam
- Faculty of Applied Science, Ho Chi Minh City University of Technology, National University Ho Chi Minh city, Vietnam
Correspondence to:
Huynh Quang Linh,
Faculty of Applied Science, Ho Chi Minh City University of Technology, National University Ho Chi Minh city, Vietnam.
Email:
huynhqlinh@hcmut.edu.vn.
Volume & Issue:
Vol. 24 No. SI1 (2021): Special issue: Recent developments and emerging trends in biomedical engineering and engineering mechanics 2021
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Page No.:
SI79-SI84
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DOI:
10.32508/stdj.v24iSI1.3904
Published:
2022-05-11
Abstract
Alzheimer’s disease is associated with a progressive intracerebral accumulation of amyloid beta (Aβ) peptides, which have different numbers of amino acids, but Aβ40 and Aβ42 are the most abundant in vivo. However, Aβ42 is more toxic than Aβ40. Thioflavin-T has been used in research to investigate amyloid beta formation, but the interaction mechanism remains unclear. In this study, using the docking method, we calculated the binding between thioflavin-T and aggregations of Aβ42, including fibril, tetramer, and dimer Aβ42. The results show that thioflavin-T binds to fibrils more strongly than soluble oligomers. The binding mechanism depends on the conformations of the assembly structures.