The Effect of Osmolytes on Protein Fibrillation
Osmolytes are small molecules that are exploited by cells as a protective system against stress conditions. They favour compact protein states which makes them stabilize globular proteins in vitro and promote folding. Conversely, this preference for compact states promotes aggregation of unstructure...
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Molecular Diversity Preservation International (MDPI)
2012
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pubmed-33177442012-04-09 The Effect of Osmolytes on Protein Fibrillation Macchi, Francesca Eisenkolb, Maike Kiefer, Hans Otzen, Daniel E. Article Osmolytes are small molecules that are exploited by cells as a protective system against stress conditions. They favour compact protein states which makes them stabilize globular proteins in vitro and promote folding. Conversely, this preference for compact states promotes aggregation of unstructured proteins. Here we combine a brief review of the effect of osmolytes on protein fibrillation with a report of the effect of osmolytes on the unstructured peptide hormone glucagon. Our results show that osmolytes either accelerate the fibrillation kinetics or leave them unaffected, with the exception of the osmolyte taurine. Furthermore, the osmolytes that affected the shape of the fibrillation time profile led to fibrils with different structure as revealed by CD. The structural changes induced by Pro, Ser and choline-O-sulfate could be due to specific osmolytes binding to the peptides, stabilizing an otherwise labile fibrillation intermediate. Molecular Diversity Preservation International (MDPI) 2012-03-21 /pmc/articles/PMC3317744/ /pubmed/22489184 http://dx.doi.org/10.3390/ijms13033801 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
repository_type |
Open Access Journal |
institution_category |
Foreign Institution |
institution |
US National Center for Biotechnology Information |
building |
NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Macchi, Francesca Eisenkolb, Maike Kiefer, Hans Otzen, Daniel E. |
spellingShingle |
Macchi, Francesca Eisenkolb, Maike Kiefer, Hans Otzen, Daniel E. The Effect of Osmolytes on Protein Fibrillation |
author_facet |
Macchi, Francesca Eisenkolb, Maike Kiefer, Hans Otzen, Daniel E. |
author_sort |
Macchi, Francesca |
title |
The Effect of Osmolytes on Protein Fibrillation |
title_short |
The Effect of Osmolytes on Protein Fibrillation |
title_full |
The Effect of Osmolytes on Protein Fibrillation |
title_fullStr |
The Effect of Osmolytes on Protein Fibrillation |
title_full_unstemmed |
The Effect of Osmolytes on Protein Fibrillation |
title_sort |
effect of osmolytes on protein fibrillation |
description |
Osmolytes are small molecules that are exploited by cells as a protective system against stress conditions. They favour compact protein states which makes them stabilize globular proteins in vitro and promote folding. Conversely, this preference for compact states promotes aggregation of unstructured proteins. Here we combine a brief review of the effect of osmolytes on protein fibrillation with a report of the effect of osmolytes on the unstructured peptide hormone glucagon. Our results show that osmolytes either accelerate the fibrillation kinetics or leave them unaffected, with the exception of the osmolyte taurine. Furthermore, the osmolytes that affected the shape of the fibrillation time profile led to fibrils with different structure as revealed by CD. The structural changes induced by Pro, Ser and choline-O-sulfate could be due to specific osmolytes binding to the peptides, stabilizing an otherwise labile fibrillation intermediate. |
publisher |
Molecular Diversity Preservation International (MDPI) |
publishDate |
2012 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317744/ |
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1611518649446694912 |