Separation of complexes of major histocompatibility class II molecules and known antigenic peptide by metal chelate affinity chromatography (J. Immunol. Methods 169 (1994) 273–285)

Nano-electrospray and microbore liquid chromatography-ion trap mass spectrometry studies of copper complexation with MHC restricted peptides

“…Interactions of peptides with alkali metal, 8,9 alkali earth metal 10,11 and transition metal [12][13][14][15] ions have been demonstrated using ESI-MS, and molecular modelling 15,16 has played an integral part in predicting metallation sites. Copper ion/ peptide complexation has also been explored for model peptides using ESI-MS 14,[17][18][19][20][21] because of the important role of copper in biochemical systems.…”

“…22 These metal-peptide interactions have been exploited for the selective separation of peptides from complex mixtures via metal chelate affinity chromatography. 16,23 Tandem mass spectrometric studies have indicated that histidine containing peptides have a particularly strong affinity for transition metals, although copper can bind to other amino acids through association with the C-terminus of the peptide. 16,24 Mass spectrometric analysis of copper/peptide complexation has, however, not been extended to naturally occurring peptides in the range of 8-22 amino acids.…”

“…16,23 Tandem mass spectrometric studies have indicated that histidine containing peptides have a particularly strong affinity for transition metals, although copper can bind to other amino acids through association with the C-terminus of the peptide. 16,24 Mass spectrometric analysis of copper/peptide complexation has, however, not been extended to naturally occurring peptides in the range of 8-22 amino acids. In this paper, we report an investigation into the formation of copper/ peptide complex ions with MHC class I and class II restricted peptides using nano-electrospray ionization and microbore LC-MS with post-column complexation.…”