期刊
PLOS ONE
卷 16, 期 10, 页码 -出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0258692
关键词
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资金
- Philippine Department of Science and Technology (DOST) Accelerated Science and Technology Human Resource Development Program (ASTHRDP)
- Nazarbayev University Faculty Development Competitive Research Grant [240919FD3938]
The study demonstrates the amphipathic nature of PHF-Tau and molecular dynamics simulations indicate that the embedded phosphocholine at the tail side results in high potential energy values with some amino acids forming H-bond interactions.
The microtubule-binding protein tau has been the center of researches concerning Alzheimer's disease (AD) due to several clinical trials of beta-amyloid therapies failing recently. The availability of the tau fibril structure from AD brain enables computational modeling studies to calculate binding affinities with different ligands. In this study, the tau paired helical filaments (PHF-Tau) (PDB ID: 5O3L) was used as receptor and interactions with the lipids: 3-alpha-cholesterol; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; and C18:1 sphingomyelin, were explored with molecular docking, molecular dynamics, and natural bond orbital analysis. Docking sites upon solvation of the protein with transferable interatomic potential-3 points reveal the amphipathic nature of PHF-Tau and molecular dynamics simulations show that the embedded phosphocholine at the tail side gives high potential energy values with some amino acids forming H-bond interactions.
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