Multiple glycosylation of de novo designed α-helical coiled coil peptides.

J.A. Falenski, U.I.M. Gerling, B. Koksch – 2010

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.

Titel
Multiple glycosylation of de novo designed α-helical coiled coil peptides.
Verfasser
J.A. Falenski, U.I.M. Gerling, B. Koksch
Datum
2010
Kennung
10.1016/j.bmc.2010.03.061
Quelle/n
Zitierweise
Bioorg. Med. Chem. 2010, 18, 3703–3706.
Art
Text
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