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Solubilization and disaggregation of polyglutamine peptides
Open accessAbstract
A method is described for dissolving and disaggregating chemically synthesized polyglutamine peptides. Polyglutamine peptides longer than about Q 20 have been reported to be insoluble in water, but dissolution in – and evaporation from ‐ a mixture of trifluoroacetic acid and hexafluoroisopropanol converts polyglutamine peptides up to at least Q 44 to a form readily soluble in aqueous buffers. This procedure also has a dramatic effect on peptides which appear to be completely soluble in water, by removing traces of aggregate that seed aggregation. The protocol makes possible solution studies—including in vitro aggregation experiments—on polyglutamine peptides with repeat lengths associated with increased risk of Huntington's Disease and other expanded CAG repeat diseases. It may also be useful in conducting reproducible, quantitative aggregation studies on other polypeptides.
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Cited by
Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
O'Nuallain, B., Williams, A. D., Westermark, P., & Wetzel, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311300200 · Cited by 423
Self-citationAggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
Yang, W. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.23.2905 · Cited by 371
Lactadherin binds to elastin--a starting point for medin amyloid formation?
Larsson, A., Peng, S., Persson, H., Rosenbloom, J., Abrams, W. R., Wassberg, E., Thelin, S., Sletten, K., Gerwins, P., & Westermark, P. (2006) · Amyloid · doi:10.1080/13506120600722530 · Cited by 50
Structure of puromycin-sensitive aminopeptidase and polyglutamine binding
Madabushi, S., Chow, K. M., Song, E. S., Goswami, A., Hersh, L. B., & Rodgers, D. W. (2023) · PLOS ONE · doi:10.1371/journal.pone.0287086 · Cited by 9
Metadata
- Authors
- Chen, S., & Wetzel, R.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2001-04
- Volume
- 10
- Issue
- 4
- Pages
- 887-891
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2074182100
- Cited by
- 182
- References
- 0
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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