Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation

Garvey, Megan, Baumann, Monika, Wulff, Melanie, Kumar, Senthil T., Markx, Daniel, Morgado, Isabel, Knüpfer, Uwe, Horn, Uwe, Mawrin, Christian, Fändrich, Marcus and Balbach, Jochen 2016, Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation, Amyloid, vol. 23, no. 2, pp. 76-85, doi: 10.3109/13506129.2016.1146989.

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Title Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation
Author(s) Garvey, Megan
Baumann, Monika
Wulff, Melanie
Kumar, Senthil T.
Markx, Daniel
Morgado, Isabel
Knüpfer, Uwe
Horn, Uwe
Mawrin, Christian
Fändrich, Marcus
Balbach, Jochen
Journal name Amyloid
Volume number 23
Issue number 2
Start page 76
End page 85
Total pages 9
Publisher Taylor & Francis
Place of publication Basingstoke, Eng.
Publication date 2016-03
ISSN 1744-2818
Keyword(s) Alzheimer’s disease
H/D-exchange
NMR
amyloid fibrils
neurodegeneration
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Medicine, General & Internal
Medicine, Research & Experimental
General & Internal Medicine
Research & Experimental Medicine
Alzheimer's disease
NUCLEAR-MAGNETIC-RESONANCE
SOLID-STATE NMR
ALZHEIMERS-DISEASE
SOLVENT PROTECTION
HYDROGEN-EXCHANGE
STRUCTURAL MODEL
3D STRUCTURE
PROTEIN
Summary OBJECTIVES: The detailed structure of brain-derived Aβ amyloid fibrils is unknown. To approach this issue, we investigate the molecular architecture of Aβ(1-40) fibrils grown in either human cerebrospinal fluid solution, in chemically simple phosphate buffer in vitro or extracted from a cell culture model of Aβ amyloid plaque formation. METHODS: We have used hydrogen-deuterium exchange (HX) combined with nuclear magnetic resonance, transmission electron microscopy, seeding experiments both in vitro and in cell culture as well as several other spectroscopic measurements to compare the morphology and residue-specific conformation of these different Aβ fibrils. RESULTS AND CONCLUSIONS: Our data reveal that, despite considerable variations in morphology, the spectroscopic properties and the pattern of slowly exchanging backbone amides are closely similar in the fibrils investigated. This finding implies that a fundamentally conserved molecular architecture of Aβ peptide fold is common to Aβ fibrils.
Language eng
DOI 10.3109/13506129.2016.1146989
Field of Research 119999 Medical and Health Sciences not elsewhere classified
1103 Clinical Sciences
1109 Neurosciences
0601 Biochemistry And Cell Biology
Socio Economic Objective 929999 Health not elsewhere classified
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2016, Informa UK
Persistent URL http://hdl.handle.net/10536/DRO/DU:30085929

Document type: Journal Article
Collection: School of Medicine
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