The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
A facile method for expression and purification of the Alzheimer’s disease‐associated amyloid β‐peptide
Open accessAbstract
We report the development of a high‐level bacterial expression system for the Alzheimer’s disease‐associated amyloid β‐peptide (Aβ), together with a scaleable and inexpensive purification procedure. Aβ(1–40) and Aβ(1–42) coding sequences together with added ATG codons were cloned directly into a Pet vector to facilitate production of Met‐Aβ(1–40) and Met‐Aβ(1–42), referred to as Aβ(Μ1–40) and Aβ(Μ1–42), respectively. The expression sequences were designed using codons preferred by Escherichia coli, and the two peptides were expressed in this host in inclusion bodies. Peptides were purified from inclusion bodies using a combination of anion‐exchange chromatography and centrifugal filtration. The method described requires little specialized equipment and provides a facile and inexpensive procedure for production of large amounts of very pure Aβ peptides. Recombinant peptides generated using this protocol produced amyloid fibrils that were indistinguishable from those formed by chemically synthesized Aβ1–40 and Aβ1–42. Formation of fibrils by all peptides was concentration‐dependent, and exhibited kinetics typical of a nucleation‐dependent polymerization reaction. Recombinant and synthetic peptides exhibited a similar toxic effect on hippocampal neurons, with acute treatment causing inhibition of MTT reduction, and chronic treatment resulting in neuritic degeneration and cell loss.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
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Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Self-citationThe 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Self-citationAmyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Self-citationAssembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
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Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
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Structural Classification of Toxic Amyloid Oligomers
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Cited by
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,440
Self-citationMolecular mechanisms of protein aggregation from global fitting of kinetic models
Meisl, G., Kirkegaard, J. B., Arosio, P., Michaels, T. C. T., Vendruscolo, M., Dobson, C. M., Linse, S., & Knowles, T. P. J. (2016) · Nature Protocols · doi:10.1038/nprot.2016.010 · Cited by 767
Self-citationBiochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease
Masters, C. L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006262 · Cited by 542
Alzheimer's disease: synaptic dysfunction and Aβ
Shankar, G. M., & Walsh, D. M. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-48 · Cited by 486
Self-citationA molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Cohen, S. I. A., Arosio, P., Presto, J., Kurudenkandy, F. R., Biverstål, H., Dolfe, L., Dunning, C., Yang, X., Frohm, B., Vendruscolo, M., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2971 · Cited by 414
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Metadata
- Authors
- Walsh, D. M., Thulin, E., Minogue, A. M., Gustavsson, N., Pang, E., Teplow, D. B., & Linse, S.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2009-02-16
- Volume
- 276
- Issue
- 5
- Pages
- 1266-1281
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1797763128
- Cited by
- 284
- References
- 10
- FWCI
- 4.13
- Type
- journal article
- Language
- en
- Open access
- green
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