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.
Falenski
Jessica A
JA
Institute of Chemistry and Biochemistry, Organic Chemistry, Freie Universität Berlin, 14195 Berlin, Germany.
Gerling
Ulla I M
UI
Koksch
Beate
B
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