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 α-helical conformation by using FT-IR spectra. The end-capping reagents for the N-terminus of the peptide were also evaluated.