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@ARTICLE{ZhangHaagen:808413,
author = {Zhang-Haagen, Bo and Biehl, Ralf and Nagel-Steger, Luitgard
and Radulescu, Aurel and Richter, Dieter and Willbold,
Dieter},
title = {{M}onomeric {A}myloid {B}eta {P}eptide in
{H}exafluoroisopropanol {D}etected by {S}mall {A}ngle
{N}eutron {S}cattering},
journal = {PLoS one},
volume = {11},
number = {2},
issn = {1932-6203},
address = {Lawrence, Kan.},
publisher = {PLoS},
reportid = {FZJ-2016-02236},
pages = {e0150267 -},
year = {2016},
abstract = {Small proteins like amyloid beta (Aβ) monomers are related
to neurodegenerative disorders by aggregation to insoluble
fibrils. Small angle neutron scattering (SANS) is a
nondestructive method to observe the aggregation process in
solution. We show that SANS is able to resolve monomers of
small molecular weight like Aβ for aggregation studies. We
examine Aβ monomers after prolonged storing in
d-hexafluoroisopropanol (dHFIP) by using SANS and dynamic
light scattering (DLS). We determined the radius of gyration
from SANS as 1.0±0.1 nm for Aβ1–40 and 1.6±0.1 nm for
Aβ1–42 in agreement with 3D NMR structures in similar
solvents suggesting a solvent surface layer with $5\%$
increased density. After initial dissolution in dHFIP Aβ
aggregates sediment with a major component of pure monomers
showing a hydrodynamic radius of 1.8±0.3 nm for Aβ1–40
and 3.2±0.4 nm for Aβ1–42 including a surface layer of
dHFIP solvent molecules.},
cin = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
(München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
ICS-1 / ICS-6},
ddc = {500},
cid = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106 /
I:(DE-Juel1)ICS-6-20110106},
pnm = {6G15 - FRM II / MLZ (POF3-6G15) / 553 - Physical Basis of
Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-553},
experiment = {EXP:(DE-MLZ)KWS2-20140101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000371274400114},
pubmed = {pmid:26919121},
doi = {10.1371/journal.pone.0150267},
url = {https://juser.fz-juelich.de/record/808413},
}