TY  - JOUR
AU  - Barz, Bogdan
AU  - Buell, Alexander K.
AU  - Nath, Soumav
TI  - Compact fibril-like structure of amyloid β-peptide (1–42) monomers
JO  - Chemical communications
VL  - 57
IS  - 7
SN  - 0009-241X
CY  - Cambridge
PB  - Soc.
M1  - FZJ-2021-05876
SP  - 947 - 950
PY  - 2021
AB  - Amyloid β (Aβ) monomers are the smallest assembly units, and play an important role in most of the individual processes involved in amyloid fibril formation. An important question is whether the monomer can adopt transient fibril-like conformations in solution. Here we use enhanced sampling simulations to study the Aβ42 monomer structural flexibility. We show that the monomer frequently adopts conformations with the N-terminus region structured very similarly to the conformation it adopts inside the fibril. This intrinsic propensity of monomeric Aβ to adopt fibril-like conformations could explain the low free energy barrier for Aβ42 fibril elongation.
LB  - PUB:(DE-HGF)16
C6  - pmid:33399148
UR  - <Go to ISI:>//WOS:000612511600025
DO  - DOI:10.1039/D0CC06607A
UR  - https://juser.fz-juelich.de/record/904306
ER  -