Improving the aqueous solubility of HCV-E2 glycoprotein epitope mimics by cyclization using POLAR hinges.

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ID: 87267
2020
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Abstract
In this research we describe the improvement of the water-solubility of cyclic epitope mimics based on the HCV E2 glycoprotein by incorporation of suitable polar hinges. The poor solubility of epitope mimics based on peptide sequences in the envelope (E2) protein hampered their synthesis and purification and made it very difficult to prepare the molecular constructs for evaluation of their bioactivity. Since changes in the amino acid composition are hardly possible in these epitope mimics in order to increase water-solubility, a polar cyclization hinge may offer a remedy leading to a significant increase of polarity and therefore water solubility. These polar hinges were applied in the synthesis of better water-soluble HCV-E2 epitopes. An azide functionality in the polar hinges allowed attachment of a tetraethylene glycol linker by Cu-catalyzed azide-alkyne cyclo-addition (CuAAC) for a convenient conjugation to ELISA plates in order to evaluate the bio-activity of the epitope mimics. The immunoassays showed that the use of more polar cyclization hinges still supported anti-HCV antibody recognition and did not negatively influence their binding. This significantly increased solubility induced by polar hinges should therefore allow for the molecular construction and ultimate evaluation of synthetic vaccine molecules.
Reference Key
meuleman2020improvingjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Meuleman, Theodorus J;Cowton, Vanessa M;Patel, Arvind H;Liskamp, Rob M J;
Journal journal of peptide science : an official publication of the european peptide society
Year 2020
DOI
10.1002/psc.3222
URL
Keywords
ELISA hepatitis c virus cyclic peptides cyclisation method epitope mimics polar hinge synthetic vaccine

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