Multiple glycosylation of de novo designed alpha-helical coiled coil peptides.
The aim of this study was to investigate the influence of multiple O-glycosylation in alpha-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six beta-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 beta-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.
Institute of Chemistry and Biochemistry, Organic Chemistry, Freie Universität Berlin, 14195 Berlin, Germany.
Jessica A
JA
Falenski
Ulla I M
UI
Gerling
Beate
B
Koksch
D002942:Circular Dichroism; D015195:Drug Design; D005690:Galactose / Q000737:chemistry*; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D006031:Glycosylation; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011489:Protein Denaturation; D055550:Protein Stability; D017433:Protein Structure, Secondary
D006020:Glycopeptides; D010455:Peptides; D005690:Galactose