Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1207243 | Journal of Chromatography A | 2008 | 4 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Kaname Ohyama, Kana Oyamada, Naoya Kishikawa, Yoshihito Ohba, Mitsuhiro Wada, Toshihide Maki, Kenichiro Nakashima, Naotaka Kuroda,