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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Main Authors: Macchi, Francesca, Eisenkolb, Maike, Kiefer, Hans, Otzen, Daniel E.
Format: Online
Language:English
Published: Molecular Diversity Preservation International (MDPI) 2012
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317744/
id pubmed-3317744
recordtype oai_dc
spelling 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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