title: Divergent behavior of glycosylated threonine and serine derivatives in solid phase peptide synthesis.
abstract: Solid phase peptide coupling of glycosylated threonine derivatives was systematically evaluated. In contrast to glycosylated serine derivatives which are highly prone to epimerization, glycosylated threonine derivatives produce only negligible amounts of epimerization. Under forcing conditions, glycosylated threonine analogs undergo β-elimination, rather than epimerization. Mechanistic studies and molecular modeling were used to understand the origin of the differences in reactivity.
authors: Chemical Biology Laboratory, National Cancer Institute, 376 Boyles Street, Building 376, Frederick, Maryland 21702, USA.
authors: Yalong
authors: Y
authors: Zhang
authors: Saddam M
authors: SM
authors: Muthana
authors: Joseph J
authors: JJ
authors: Barchi
authors: Jeffrey C
authors: JC
authors: Gildersleeve
mesh_terms: D006031:Glycosylation; D015394:Molecular Structure; D012694:Serine / Q000737:chemistry*; D060327:Solid-Phase Synthesis Techniques; D013329:Structure-Activity Relationship; D013912:Threonine / Q000737:chemistry*
chemical_list: D013912:Threonine; D012694:Serine