Abstract
The monomer and the oligomers of a bioactive cyclic peptide were separated using micellar electrokinetic chromatography (MEKC) in order to determine if oligomeric forms of the peptide were present or not. Producing cyclic peptides involves the formation of an intramolecular disulphide bridge. During cyclisation, intermolecular disulphide bonds may be formed, thus resulting in unwanted oligomeric forms of the peptide. The cyclic peptide studied was shown by size-exclusion chromatography to be capable of forming a monomer, dimer, trimer and tetramer. The higher resolution MEKC provides was needed to separate further components of the oligomers. In phosphate buffer pH 7.5 containing sodium dodecyl sulphate 20 species could be separated in 18 min. Both linear and cyclic oligomeric isomers appeared to be present.
Published Version
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