title: Probing the stability of nonglycosylated wild-type erythropoietin protein via reiterative alanine ligations.
abstract: Nonglycosylated erythropoietin bearing acetamidomethyl protecting groups at the cysteine residues has been synthesized via chemical methods. Alanine ligation was used to assemble four peptide fragments, themselves prepared by solid phase peptide synthesis. This work outlines a route for the synthesis of homogeneous glycosylated erythropoietin.
authors.affiliation: Bio-Organic Chemistry Laboratory, Molecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA.
authors.forename: John A
authors.initials: JA
authors.lastname: Brailsford
authors.forename: Samuel J
authors.initials: SJ
authors.lastname: Danishefsky
mesh_terms: D000409:Alanine / Q000737:chemistry*; D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D003545:Cysteine / Q000737:chemistry*; D004921:Erythropoietin / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D008956:Models, Chemical; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D009844:Oligosaccharides; D010446:Peptide Fragments; D004921:Erythropoietin; D003545:Cysteine; D000409:Alanine