Tuning the conformation properties of a peptide by glycosylation and phosphorylation.
We have deployed the alpha-helical hairpin peptide (alpha-helix/turn/alpha-helix) and used it as a model system to explore how glycosylation and phosphorylation might affect the conformational properties of the peptide. The native conformations of the modified peptides in buffer solution have been compared with that of the wild-type peptide by nuclear magnetic resonance spectroscopy. Circular dichroism spectroscopy was used to probe the effects of an O-linked beta-GlcNAc and a phosphate group on the overall folding stability of the peptide. Finally, the rate of fibrillogenesis was used to infer the effects of these chemical modifications on the alpha-to-beta transition as well as the rate of nucleation of amyloidogenesis.
Institute of Chemistry, Academia Sinica, Taipei, Taiwan, ROC.
Fu-Cheng
FC
Liang
Rita P-Y
RP
Chen
Chun-Cheng
CC
Lin
Kuo-Ting
KT
Huang
Sunney I
SI
Chan
D000117:Acetylglucosamine / Q000737:chemistry; D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure; D006031:Glycosylation; D019077:Helix-Turn-Helix Motifs; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D015202:Protein Engineering; D012996:Solutions; D013696:Temperature
D000682:Amyloid; D010455:Peptides; D012996:Solutions; D000117:Acetylglucosamine