Journal Article FZJ-2016-02236

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Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering

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2016
PLoS Lawrence, Kan.

PLoS one 11(2), e0150267 - () [10.1371/journal.pone.0150267]

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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.

Keyword(s): Health and Life (1st) ; Health and Life (1st) ; Biology (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II)
  2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
  3. Neutronenstreuung (ICS-1)
  4. Strukturbiochemie (ICS-6)
Research Program(s):
  1. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
  2. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)
Experiment(s):
  1. KWS-2: Small angle scattering diffractometer (NL3ao)

Appears in the scientific report 2016
Database coverage:
Medline ; Creative Commons Attribution CC BY 4.0 ; DOAJ ; OpenAccess ; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record
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The record appears in these collections:
Institute Collections > JCNS > JCNS-FRM-II
Document types > Articles > Journal Article
Institute Collections > JCNS > JCNS-1
Institute Collections > IBI > IBI-8
Institute Collections > IBI > IBI-7
Workflow collections > Public records
Workflow collections > Publication Charges
ICS > ICS-1
ICS > ICS-6
Publications database
Open Access

 Record created 2016-04-12, last modified 2024-06-19