P. Hansen et G. Lindeberg, PURIFICATION OF TRYPTOPHAN CONTAINING SYNTHETIC PEPTIDES BY SELECTIVEBINDING OF THE ALPHA-AMINO GROUP TO IMMOBILIZED METAL-IONS, Journal of chromatography, 662(2), 1994, pp. 235-241
Immobilised metal ion affinity chromatography (IMAC) based on selectiv
e binding via the alpha-amino group to Cu2+ and Ni2+ ions has been use
d to purify tryptophan containing synthetic peptides. A free alpha-ami
no group, serving as an affinity handle, is present only in the target
peptide when the peptides are synthesised by the solid-phase method a
nd remaining amino groups after each coupling step are blocked by acet
ylation. A free alpha-amino group is necessary to retain the peptide o
n the column. The tryptophan residue may contribute to the binding onl
y if the peptide is simultaneously anchored via the alpha-amino group.