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000889731 1001_ $$0P:(DE-Juel1)132024$$aStrodel, Birgit$$b0$$eCorresponding author$$ufzj
000889731 245__ $$aAmyloid aggregation simulations: challenges, advances and perspectives
000889731 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2021
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000889731 520__ $$aIn 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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