How the α-hydroxymethylserine residue stabilizes oligopeptide complexes with nickel(II) and copper(II) ions

Molecular mechanisms in nickel carcinogenesis: modeling Ni(II) binding site in histone H4.

“…Hence, a lower pK a (NH im + ) value will be associated with a lower degree of electron donation to the metal ion, which will be reflected in a lower value for pK a amide. Therefore, the lower the basicity of the N(3), the more simple the deprotonation, promoted by metal ions, of amide nitrogens, resulting in an enhancement of π-electron contribution to the metal amide nitrogen bond compared with Boc-AGGH or other simple peptides (37).…”

Nickel Ion Complexes of Amino Acids and Peptides

“…It has been reported that the insertion of HmS residues into di-or tripeptides, HmS-His and HmS-Hms-His, signifi cantly increases both the copper(II) and nickel(II) binding capacity of these ligands compared with those of GlyHis or GlyGlyHis [100,101]. (Aminoalkyl)phosphonic and (aminoalkyl)phosphinic acids are the phosphorous analogs of the naturally occurring amino acids and their insertion into the peptide backbone provides an effi cient way for the modifi cation of the acid-base and complexing properties of the oxygen donor atoms of peptide ligands.…”

Ab initio Calculations for Exploring Metal Ion-(Gly-Gly-His) Complexes

“…1,2,6,13 In this study, our attention is focused on the interaction between the oligopeptide of three amino acid residues (GlyGly-His) and metal ion without solvent effect. (The response of the Gly-Gly-His modified electrode to Cu 2+ ion was measured as a current in the solution experiment of Fisher et al.…”

“…2 Theoretical approaches about metal-oligopeptide structure and metal-ligand coordination geometry have been also performed by molecular dynamics simulations and ab initio calculations. [9][10][11][12][13] Studies have focused on the structural data of metal ion-ligand complexes. Four-coordination geometries were mainly discussed because they are most frequently encountered in the metal-binding sites of metalloproteins.…”

“…10,11 Several groups reported the interactions between the special oligopeptides of three or four amino acid residues and metal ion because those oligopeptides are principally capable of providing the saturated (four electron donor atoms) equatorial binding site. 1,2,6,13 In this study, our attention is focused on the interaction between the oligopeptide of three amino acid residues (GlyGly-His) and metal ion without solvent effect. (The response of the Gly-Gly-His modified electrode to Cu 2+ ion was measured as a current in the solution experiment of Fisher et al.…”