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• W2912755692 abstract "The amyloid β (Aβ) fibril is a hallmark of Alzheimer’s disease (AD) and has therefore served as an important target for early diagnosis of AD. The Pittsburgh Compound-B (PiB) is one of the most famous positron emission tomography (PET) tracers commonly used for in vivo detection of Aβ fibrils. Many theoretical studies have predicted the existence of various core binding sites with different microenvironments for probes binding to the Aβ fibril. However, little attention has been devoted to how the probes actually penetrate into the different core binding sites. In this study, an integrated molecular modeling scheme is used to study the penetration of PiB into the core binding sites of the Aβ1–42 fibril structure recently obtained by cryogenic electron microscopy. We find that there are two core binding sites for PiB with dramatic differences in cavity size and microenvironment properties, and furthermore that the penetration of PiB into site-1 is energetically prohibitive, whereas the penetration into site-2 is much more favorable. Therefore, the binding capacity at site-2 may be larger than that at site-1 despite its lower binding affinity. Our results thus suggest that site-2 may be a major binding site for PiB binding to Aβ fibril and emphasize the importance to adopt a full dynamical picture when studying tracer–fibril binding problems in general, something that in turn can be used to guide the development of tracers with higher affinity and selectivity for the Aβ fibril." @default.
• W2912755692 created "2019-02-21" @default.
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• W2912755692 date "2019-01-30" @default.
• W2912755692 modified "2023-10-01" @default.
• W2912755692 title "Free Energy Profile for Penetration of Pittsburgh Compound-B into the Amyloid β Fibril" @default.
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• W2912755692 doi "https://doi.org/10.1021/acschemneuro.8b00662" @default.
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