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Published on: June 7, 2015
Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel
Meder Kamalov1, Hanspeter Kählig2, Christian Rentenberger3
1Institute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Strasse 38, 1090, Vienna, Austria.
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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