Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel

  • Sci Rep. 2019 Feb 25;9(1):2696. doi: 10.1038/s41598-019-39148-8.
Meder Kamalov  1 ,  Hanspeter Kählig  2 ,  Christian Rentenberger  3 ,  Alexander R M Müllner  4 ,  Herwig Peterlik  4 ,  Christian F W Becker  5
Affiliations
  • 1. Institute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Strasse 38, 1090, Vienna, Austria.
  • 2. Institute of Organic Chemistry, Faculty of Chemistry, University of Vienna, Währinger Strasse 38, 1090, Vienna, Austria.
  • 3. Physics of Nanostructured Materials, Faculty of Physics, University of Vienna, Boltzmanngasse 5, 1090, Vienna, Austria.
  • 4. Dynamics of Condensed Systems, Faculty of Physics, University of Vienna, Boltzmanngasse 5, 1090, Vienna, Austria.
  • 5. Institute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Strasse 38, 1090, Vienna, Austria. [email protected].
PMID: 30804439 DOI: 10.1038/s41598-019-39148-8
Abstract

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.

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