Journal Article

FZJ-2021-00352

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Amyloid aggregation simulations: challenges, advances and perspectives

Strodel, B. (Corresponding author)FZJ*

2021
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: http://hdl.handle.net/2128/26820  doi:10.1016/j.sbi.2020.10.019

Abstract: 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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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)
2. 5244 - Information Processing in Neuronal Networks (POF4-524) (POF4-524)

Appears in the scientific report 2021

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Database coverage:
; ; ; BIOSIS Previews ; BIOSIS Reviews Reports And Meetings ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; JCR ; Nationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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