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001     889731
005     20230111074229.0
024 7 _ |a 10.1016/j.sbi.2020.10.019
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100 1 _ |a Strodel, Birgit
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245 _ _ |a Amyloid aggregation simulations: challenges, advances and perspectives
260 _ _ |a Amsterdam [u.a.]
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520 _ _ |a In amyloid aggregation diseases soluble proteins coalesce intoa wide array of undesirable structures, ranging througholigomers and prefibrillar assemblies to highly ordered amyloidfibrils and plaques. Explicit-solvent all-atom moleculardynamics (MD) simulations of amyloid aggregation have beenperformed for almost 20 years, revealing valuable informationabout this phenomenon. However, these simulations arechallenged by three main problems. Firstly, current force fieldsmodeling amyloid aggregation are insufficiently accurate.Secondly, the protein concentrations in MD simulations areusually orders of magnitude higher than those used in vitro orfound in vivo, which has direct consequences on theaggregates that form. Finally, the third problem is the wellknowntime-scale limit of MD simulations. In this review Ihighlight recent approaches to overcome these threelimitations.
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773 _ _ |a 10.1016/j.sbi.2020.10.019
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|y 2021
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856 4 _ |u https://juser.fz-juelich.de/record/889731/files/Amyloid%20aggregation%20simulations%20challenges%2C%20advances%20and%20perspectives-1.pdf
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