TY  - JOUR
AU  - Strodel, Birgit
TI  - Amyloid aggregation simulations: challenges, advances and perspectives
JO  - Current opinion in structural biology
VL  - 67
SN  - 0959-440X
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - FZJ-2021-00352
SP  - 145 - 152
PY  - 2021
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 33279865
UR  - <Go to ISI:>//WOS:000647703900007
DO  - DOI:10.1016/j.sbi.2020.10.019
UR  - https://juser.fz-juelich.de/record/889731
ER  -