Preparation and characterization of poly(l-phenylalanine) chiral stationary phases with varying peptide length.
Three new chiral stationary phases with different lengths of l-phenylalanine peptide were prepared by solid-phase synthesis with tert-butoxycarbonyl (Boc)-l-phenylalanine on silica. The effect of phenylalanine peptide length on enantioselectivity was studied. The best separation of R/S-warfarin was achieved by the chiral stationary phase with intermediate peptide length. These stationary phases were found to exist mainly in alpha-helical conformation by using FT-IR spectra. The end-capping reagents for the N-terminus of the peptide were also evaluated.
Ohyama
Kaname
K
Department of Environmental and Pharmaceutical Sciences, Course of Pharmaceutical Sciences, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan.
Oyamada
Kana
K
Kishikawa
Naoya
N
Ohba
Yoshihito
Y
Wada
Mitsuhiro
M
Maki
Toshihide
T
Nakashima
Kenichiro
K
Kuroda
Naotaka
N
D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D010455:Peptides / Q000138:chemical synthesis; D010649:Phenylalanine / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry; D013237:Stereoisomerism; D014859:Warfarin / Q000302:isolation & purification*
D010455:Peptides; D010649:Phenylalanine; D014859:Warfarin; D012822:Silicon Dioxide