0000000000003709
AUTHOR
Hans Brückner
Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density.
As part of further investigations on the characterization of the ligand-induced conformational stabilization of peptides, two series of n-alkyldimethylsilyl bonded silicas have been prepared. In series A the n-alkyl chain length, n, of the bonded phase was varied between 1 and 20 carbon atoms at a constant ligand density. In series B the ligand density, alpha exp, was gradually changed from 0 to 4.1 mumol/m2 on a C1, C4, C6, C8 and C18 bonded phase. The retention behaviour of four peptides of the paracelsin family were examined under isocratic conditions, using a ternary mobile phase of water-methanol-acetonitrile (22:39:39, v/v/v). Plots of k' versus n showed pronounced maxima between n = …
Isolation and structural characterization of polypeptide antibiotics of the peptaibol class by high-performance liquid chromatography with field desorption and fast atom bombardment mass spectrometry
Abstract A number of polypeptide antibiotics of the peptaibol class, i.e., trichotoxin, alamethicin, suzukacillin, hypelcin and paracelsin, have been separated into components and isolated by high-performance liquid chromatography on spherical, porous octadecylsilyl bonded phases. All peptaibols were found to reveal a strong microheterogeneity due to single or multiple amino acid exchange. Most of the closely related and partially isobaric sequence analogue could be resolved using mixed alcohol—water eluents. As demonstrated by the structure analysis of the paracelsins and the main component of trichotoxin A-50, high-performance liquid chromatography with field desorption and fast atom bomb…