Silyl linker-based approach to the solid-phase synthesis of Fmoc glycopeptide thioesters.
An efficient solid-phase synthesis of Fmoc (glyco)peptide thioesters is described. Fmoc x Ser x OAll and Fmoc x Thr x OAll bound to resin with a silyl ether linker were deallylated by Pd(0) catalysis and condensed with thiophenol, benzyl mercaptane, and ethyl 3-mercaptopropionate by activation with DCC/HOBt. The thioesters were released from the resin either by treatment with CsF-AcOH or by acidic hydrolysis. The effectiveness of this silyl linker strategy is further demonstrated by the synthesis of more complex (glyco)peptide thioesters 25, 26 and 27 involving N-->C and C-->N peptide elongation.
Ishii
Akira
A
Department of Applied Biochemistry, Tokai University, Hiratsuka-shi, Kanagawa, Japan.
Hojo
Hironobu
H
Nakahara
Yuko
Y
Ito
Yukishige
Y
Nakahara
Yoshiaki
Y
D004952:Esters / Q000138:chemical synthesis*; D005449:Fluorenes / Q000737:chemistry*; D006020:Glycopeptides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D012821:Silanes / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D004952:Esters; D005449:Fluorenes; D006020:Glycopeptides; D012821:Silanes; D013438:Sulfhydryl Compounds