Multiple glycosylation of de novo designed α-helical coiled coil peptides |
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Authors: | Jessica A Falenski Ulla IM Gerling Beate Koksch |
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Institution: | Institute of Chemistry and Biochemistry, Organic Chemistry, Freie Universität Berlin, 14195 Berlin, Germany;Max-Planck-Institute for Molecular Physiology, Dept of Chemical Biology, Otta-Hahn-Strasse 11, 44227 Dortmund, Germany |
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Abstract: | The aim of this study was to investigate the influence of multiple O-glycosylation in α-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six β-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil helix. Surprisingly, circular dichroism spectroscopy showed no unfolding of the coiled coil structure for all glycopeptides. Thermally induced denaturations reveal a successive but relative low destabilization of the coiled coil structure upon introduction of β-galactose residues. These first results indicate that O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies. |
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