SEPARATION OF PEPTIDES HAVING STRUCTURES AND DERIVATIVES OF MIMOSINE, A NONPROTEINOGENIC AMINO ACID, BY A NOVEL REVERSE-PHASE HPLC COLUMN PACKED WITH WIDE-PORE SILICA

摘要

To elucidate the mechanisms of the self-assembly and understand the molecular basis of the pathogenesis of conformational changes of proteins, β-amyloid or prion protein related peptides are indispensable materials. Hence, these peptides are known lo have β-sheel rich structures that lend to cause difficulty in syntheses, as well as characterization by the conventional solid-phase assembly with reversed-phase columns. In general, reversed-phase HPLC combined with on-line mass spectrometry (LCMS) is routinely used for analyses and purification of resulting crude peptides and is carried out using preparative scale HPLC-columns. However, for such peptides, conventional CI 8 columns often give broad-peaks. We have improved separation procedures using a novel column packed with wide-pore silica having hydrophilic properties thai gave separation of structural confor-mers with improved profiles. Thus, we have prepared several peptides for conformational studies. The same column also offers advantages for the chiral analysis of mimosine, a nonproleinogenic amino acid, which cannot be separated by the conventional CI 8 columns. Supplemental materials are available for this article. Go lo the publisher's online edition of the Journal of Liquid Chromatography and Related Technologies lo view the supplemental file.