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Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel
Here we show that the well-known ovalbumin epitope SIINFEKL that is routinely used to stimulate ovalbumin-specific T cells and to test new vaccine adjuvants can form a stable hydrogel. We investigate properties of this hydrogel by a range of spectroscopic and imaging techniques demonstrating that th...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6390181/ https://www.ncbi.nlm.nih.gov/pubmed/30804439 http://dx.doi.org/10.1038/s41598-019-39148-8 |
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author | Kamalov, Meder Kählig, Hanspeter Rentenberger, Christian Müllner, Alexander R.M. Peterlik, Herwig Becker, Christian F. W. |
author_facet | Kamalov, Meder Kählig, Hanspeter Rentenberger, Christian Müllner, Alexander R.M. Peterlik, Herwig Becker, Christian F. W. |
author_sort | Kamalov, Meder |
collection | PubMed |
description | Here we show that the well-known ovalbumin epitope SIINFEKL that is routinely used to stimulate ovalbumin-specific T cells and to test new vaccine adjuvants can form a stable hydrogel. We investigate properties of this hydrogel by a range of spectroscopic and imaging techniques demonstrating that the hydrogel is stabilized by self-assembly of the peptide into nanofibres via stacking of β-sheets. As peptide hydrogels are known to stimulate an immune response as adjuvants, the immunoactive properties of the SIINFEKL peptide may also originate from its propensity to self-assemble into a hydrogel. This finding requires a re-evaluation of this epitope in adjuvant testing. |
format | Online Article Text |
id | pubmed-6390181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63901812019-02-28 Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel Kamalov, Meder Kählig, Hanspeter Rentenberger, Christian Müllner, Alexander R.M. Peterlik, Herwig Becker, Christian F. W. Sci Rep Article Here we show that the well-known ovalbumin epitope SIINFEKL that is routinely used to stimulate ovalbumin-specific T cells and to test new vaccine adjuvants can form a stable hydrogel. We investigate properties of this hydrogel by a range of spectroscopic and imaging techniques demonstrating that the hydrogel is stabilized by self-assembly of the peptide into nanofibres via stacking of β-sheets. As peptide hydrogels are known to stimulate an immune response as adjuvants, the immunoactive properties of the SIINFEKL peptide may also originate from its propensity to self-assemble into a hydrogel. This finding requires a re-evaluation of this epitope in adjuvant testing. Nature Publishing Group UK 2019-02-25 /pmc/articles/PMC6390181/ /pubmed/30804439 http://dx.doi.org/10.1038/s41598-019-39148-8 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Kamalov, Meder Kählig, Hanspeter Rentenberger, Christian Müllner, Alexander R.M. Peterlik, Herwig Becker, Christian F. W. Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title | Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title_full | Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title_fullStr | Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title_full_unstemmed | Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title_short | Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel |
title_sort | ovalbumin epitope siinfekl self-assembles into a supramolecular hydrogel |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6390181/ https://www.ncbi.nlm.nih.gov/pubmed/30804439 http://dx.doi.org/10.1038/s41598-019-39148-8 |
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