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@ARTICLE{Barz:819511,
author = {Barz, Bogdan and Strodel, Birgit},
title = {{U}nderstanding {A}myloid-β {O}ligomerization at the
{M}olecular {L}evel: {T}he {R}ole of the {F}ibril {S}urface},
journal = {Chemistry - a European journal},
volume = {22},
number = {26},
issn = {0947-6539},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2016-05154},
pages = {8768 - 8772},
year = {2016},
abstract = {The aggregation of the amyloid β-peptide into fibrils is a
complex process that involves mechanisms such as primary and
secondary nucleation, fibril elongation and fibril
fragmentation. Some of these processes generate neurotoxic
Aβ oligomers, which are involved in the development of
Alzheimer's disease. Recent experimental studies have
emphasized the role of the fibril as a catalytic surface for
the production of highly toxic oligomers during secondary
nucleation. By using molecular dynamics simulations, we show
that it is the hydrophobic fibril region that causes the
structural changes required for catalyzing the formation of
β-sheet-rich Aβ1-42 oligomers on the fibril surface. These
results reveal, for the first time, the molecular basis of
the secondary nucleation pathway.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {553 - Physical Basis of Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-553},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000380270500009},
pubmed = {pmid:27135646},
doi = {10.1002/chem.201601701},
url = {https://juser.fz-juelich.de/record/819511},
}