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  Osmolytes modulate polyglutamine aggregation in a sequence dependent manner

Saha, I., Singh, V., Burra, G., & Thakur, A. K. (2018). Osmolytes modulate polyglutamine aggregation in a sequence dependent manner. Journal of Peptide Science, 24(8-9): UNSP e3115. doi:10.1002/psc.3115.

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Genre: Journal Article

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 Creators:
Saha, Itika1, Author              
Singh, Virender2, Author
Burra, Gunasekhar2, Author
Thakur, Ashwani Kumar2, Author
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              

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Free keywords: Huntington's disease, osmolytes, polyglutamine aggregation
 Abstract: Osmolytes stabilize protein structure and suppress protein aggregation. The mechanism of how osmolytes impact polyglutamine (polyQ) aggregation implicated in Huntington's disease was studied. By using a reverse‐phase chromatography assay, we show that methylamines‐trimethylamine N‐oxide and betaine are generic in enhancing polyQ aggregation, while a disaccharide trehalose and an amino acid citrulline moderately retard polyQ aggregation in a sequence specific manner. Despite the altered kinetics, the fundamental nucleation mechanism of polyQ aggregation and the nature of end stage aggregates remains unaffected. These results highlight the importance of using osmolytes as modulatory agents of polyQ aggregation.

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 Dates: 2018-07
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000443231500010
DOI: 10.1002/psc.3115
 Degree: -

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Title: Journal of Peptide Science
  Other : J. Peptide Sci.
Source Genre: Journal
 Creator(s):
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Publ. Info: Chichester, West Sussex, UK : John Wiley & Sons
Pages: - Volume / Issue: 24 (8-9) Sequence Number: UNSP e3115 Start / End Page: - Identifier: ISSN: 1075-2617
CoNE: https://pure.mpg.de/cone/journals/resource/954925604784