Racemization-free synthesis of C-terminal cysteine-peptide using 2-chlorotrityl resin.
We investigated the effects of bases, resins, and S-protecting groups on the extent of racemization at the C-terminal cysteine during Fmoc-based(Fmoc=fluoren-9-yl-methoxy-carbonyl) solid phase peptide synthesis. The use of 2-chlorotrityl resin was most effective in suppressing the racemization caused by the base treatment for Fmoc-cleavage. Somatostatin was successfully synthesized with practically no racemization using 2-chlorotrityl resin by Fmoc-chemistry.
Fujiwara
Y
Y
Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Japan.
Akaji
K
K
Kiso
Y
Y
D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000737:chemistry*; D005449:Fluorenes; D007202:Indicators and Reagents; D007475:Ion Exchange Resins; D010455:Peptides / Q000138:chemical synthesis*; D013237:Stereoisomerism; D014320:Triphenylmethyl Compounds
D005449:Fluorenes; D007202:Indicators and Reagents; D007475:Ion Exchange Resins; D010455:Peptides; D014320:Triphenylmethyl Compounds; C071065:2-chlorotrityl chloride; C054007:1-(9-fluorenyl)methyl chloroformate; D003545:Cysteine