Synthesis of truncated analogues for studying the process of glycosyl phosphatidylinositol modification.
Many eukaryotic proteins are modified with a glycosylphosphatidylinositol (GPI) anchor at their C-termini. This post-translational modification causes these proteins to be noncovalently tethered to the plasma membrane. The synthesis of truncated GPI anchor analogues is reported; these compounds were designed for use as soluble substrates for GPI transamidase (GPI-T), the enzyme that appends the GPI anchor onto proteins.
John
Franklin
F
Department of Chemistry, 5101 Cass Avenue, Wayne State University, Detroit, Michigan 48202, USA.
Hendrickson
Tamara L
TL
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D017261:Glycosylphosphatidylinositols / Q000737:chemistry*; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000737:chemistry*
D017261:Glycosylphosphatidylinositols; D010716:Phosphatidylinositols