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• W3116222783 endingPage "349" @default.
• W3116222783 startingPage "349" @default.
• W3116222783 abstract "In recent years, it has been realized that the tau protein is a key player in multiple neurodegenerative diseases. Positron emission tomography (PET) radiotracers that bind to tau filaments in Alzheimer’s disease (AD) are in common use, but PET tracers binding to tau filaments of rarer, age-related dementias, such as Pick’s disease, have not been widely explored. To design disease-specific and tau-selective PET tracers, it is important to determine where and how PET tracers bind to tau filaments. In this paper, we present the first molecular modelling study on PET probe binding to the structured core of tau filaments from a patient with Pick’s disease (TauPiD). We have used docking, molecular dynamics simulations, binding-affinity and tunnel calculations to explore TauPiD binding sites, binding modes, and binding energies of PET probes (AV-1451, MK-6240, PBB3, PM-PBB3, THK-5351 and PiB) with TauPiD. The probes bind to TauPiD at multiple surface binding sites as well as in a cavity binding site. The probes show unique surface binding patterns, and, out of them all, PM-PBB3 proves to bind the strongest. The findings suggest that our computational workflow of structural and dynamic details of the tau filaments has potential for the rational design of TauPiD specific PET tracers." @default.
• W3116222783 created "2021-01-05" @default.
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• W3116222783 date "2020-12-31" @default.
• W3116222783 modified "2023-10-18" @default.
• W3116222783 title "Pick’s Tau Fibril Shows Multiple Distinct PET Probe Binding Sites: Insights from Computational Modelling" @default.
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• W3116222783 doi "https://doi.org/10.3390/ijms22010349" @default.
• W3116222783 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7796283" @default.
• W3116222783 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33396273" @default.
• W3116222783 hasPublicationYear "2020" @default.
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