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Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation.
- Source :
-
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis [Amyloid] 2016 Jun; Vol. 23 (2), pp. 76-85. Date of Electronic Publication: 2016 Mar 14. - Publication Year :
- 2016
-
Abstract
- 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.<br />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.<br />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.
- Subjects :
- Amyloid cerebrospinal fluid
Amyloid beta-Peptides cerebrospinal fluid
Buffers
Cell Line
Conserved Sequence
Deuterium Exchange Measurement
Humans
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments cerebrospinal fluid
Phosphates cerebrospinal fluid
Phosphates chemistry
Plaque, Amyloid chemistry
Protein Conformation
Protein Folding
Solutions
Amyloid chemistry
Amyloid beta-Peptides chemistry
Models, Biological
Peptide Fragments chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-2818
- Volume :
- 23
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
- Publication Type :
- Academic Journal
- Accession number :
- 26972581
- Full Text :
- https://doi.org/10.3109/13506129.2016.1146989