Separation of polymyxins and octapeptins by high-performance liquid chromatography

✍ Scribed by Shigeru Terabe; Ryusei Konaka; Jun'ichi Shoji

• Book ID: 104144004
• Publisher: Elsevier Science
• Year: 1979
• Tongue: English
• Weight: 611 KB
• Volume: 173
• Category: Article
• ISSN: 1873-3778
• DOI: 10.1016/s0021-9673(00)92299-4

✦ Synopsis

Seventeen decapeptide antibiotics of the polymyxin group and nine octapeptide antibiotics of the octapeptin group have been successfully separated on a commercial reversed-phase material with tartrate buffer-acetonitrile containing sodium I-butanesulphonate and sodium sulphate as the mobile phase. 'All of the components of EM49 (a complex of octapeptins A and B) were preparatively separated by use of a large-diameter column, and the structures of two new components, named octapeptins Al and Ba, were deduced from the results of the fatty acid and amino acid analyses. INTRODUCf'ION Polymyxins (Table I), a group of polypeptide antibiotics produced by strains of Bacillus polymyxa and related species, have a general structure composed of a cyclic heptapeptide moiety and a side-chain consisting of a tripeptide with a fatty acyl residue. A large number of compounds, which are heterogeneous in acyl and/or amino acid residues, belonging to the polymyxin famiay have been reviewed by Vogler and Studer' and Shoji2. All of the polymyxins reported to date can be separated into single components by a counter-current distribution method3 or thin-layer chromatography*. -Octapeptins (Table II) have structures similar to those of polymyxins but the side-chains consist of only one amino acid with a fatty acyl residue. EM49' (later named octapeptin6) has been separated into four major components, EM49a, EM49& EM49y and EM496, on a CM-cellulose column, but both EM49a and EM496 are :::till complexes7~8. It is considered that the complete separation of these peptides by high-Fzrformance liquid chromatography (HPLC) is very useful for identifying these .*?tibiotics, for determining the relative contents of the components and for examining :'le purity. Recently a few papers have appeared on the separation of peptide anti-