Studies on cyclic peptides related to gratisin by reversed-phase high-performance liquid chromatography.
The chromatographic behaviour of several synthetic peptides related to the antibiotic peptide gratisin was investigated using reversed-phase high-performance liquid chromatography. The influence of the concentration of the peptides, column temperature and flow-rate on the chromatographic separation was examined. Of these peptides, some analogues with the D-X-D-Y-L-Pro or L-Pro-D-X-D-Y sequences and strong activities gave double peaks in the chromatogram. The isomeric conformers were separated from each of the double peaks and were in equilibrium with each other at low temperatures. It is proposed that the presence of the sequences of D-X-D-Y-L-Pro and L-Pro-D-X-D-Y in these peptides gives rise to the stabilization and various degrees of hydrophobicity of their conformers.
Tamaki
M
M
Department of Chemistry, Faculty of Science, Toho University, Chiba, Japan.
Akabori
S
S
Muramatsu
I
I
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D010455:Peptides; D010456:Peptides, Cyclic / Q000737:chemistry; D013696:Temperature
D000900:Anti-Bacterial Agents; D010455:Peptides; D010456:Peptides, Cyclic; C033282:gratisin