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Updated: Jan 23, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Experimental and computational studies of monovalent metal cation-peptide interactions in [M·GlyGlyHis]+ (M = Li, Na,
1Division of Science, Mathematics, and Technology, Governors State University, University Park 60484-0975, IL, USA.
Abstract:
[M·GlyGlyHis]+ (M = Li, Na, K, Rb, Cs, and Ag) complexes were generated using the electrospray ionization method and were subjected to collision-induced dissociation. Metal ion loss is the primary dissociation channel for [Cs·GlyGlyHis]+ whereas other complexes yield metal-bound peptide sequence ions and dehydrated ions as the main products. [Li·GlyGlyHis]+ and [Ag·GlyGlyHis]+ also generate product ions that are not observed for other complexes. Density functional theory calculations suggest that metal ion-peptide ligand interaction occurs through covalent interactions in [Li·GlyGlyHis]+ and [Ag·GlyGlyHis]+, and through electrostatic attraction in [Na·GlyGlyHis]+, [K·GlyGlyHis]+, [Rb·GlyGlyHis]+, and [Cs·GlyGlyHis]+. The calculations also suggest that fragmentation behavior of these complexes is affected by charge transfer to the ligand and ion-ligand interaction energy, and to a lesser extent by the ion size.
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