• Publications
  • Influence
Copper(II) complexes of oligopeptides containing aspartyl and glutamyl residues. Potentiometric and spectroscopic studies.
Copper(II) complexes of di-, tri- and tetra-peptides built up from Asp and/or Glu residues were studied by potentiometric and various spectroscopic techniques including UV-visible, circular dichroism
Thermodynamic and structural characterization of the macrochelates formed in the reactions of copper(II) and zinc(II) ions with peptides of histidine
Abstract Copper(II) complexes of the peptides Ac-HisSarHis-NH2, Ac-HisSarHisSarHis-NH2 and Ac-HisSarHisSarHisSarHis-NH2 have been studied by potentiometric, UV–Vis, CD and EPR spectroscopic methods.
Transition metal complexes of L-cysteine containing di- and tripeptides.
TLDR
Formation of the stable bis-complexes with [S,O] coordination mode is characteristic for cobalt(II), zinc(II, and cadmium(II) ions.
Isolation and complexation of the cis isomer of the pendant arm macrocycle 6,13-dimethyl-1,4,8,11-tetraazacyclotetradecane-6,13-diamine
The cis isomer of the pendant arm macrocyclic hexaamine 6,13-dimethyl-1,4,8,11-tetraazacyclotetradecane-6,13-diamine (L2) has been isolated for the first time. The ligand has been complexed with
Peptides as complexing agents: Factors influencing the structure and thermodynamic stability of peptide complexes
Abstract Peptides are versatile and powerful ligands to form stable complexes with the great majority of metal ions. The outstanding stability of peptide complexes is, however, linked to the
EPR AND POTENTIOMETRIC REINVESTIGATION OF COPPER(II) COMPLEXATION WITH SIMPLE OLIGOPEPTIDES AND RELATED COMPOUNDS
Abstract The coordination modes of Cu(II) to Di-, Tri-, and Tetra-glycine and related ligands were investigated, within the entire measurable pH range and over a wide range of ligand excess, by means
Thermodynamic and Structural Characterization of the Copper(II) Complexes of Peptides Containing Both Histidyl and Aspartyl Residues
TLDR
Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules.
Coordination, redox properties and SOD activity of Cu(II) complexes of multihistidine peptides.
TLDR
The results of electrochemical and SOD activity measurements of copper(II) complexes of terminally protected multihistidine peptides that may mimic the active site of CuZnSOD enzyme confirm that the thermodynamic stabilities increase with the increasing number of histidyl residues in the amino acid sequence, the stability order can be finely tuned by the number and quality of amino acids between histidine residues.
Cadmium(II) complexes of amino acids and peptides.
TLDR
Stability constants of the cadmium(II) complexes of both L-cysteine and its peptides and related ligands are significantly higher than those of the zinc(II), except the complexes of thiolate ligands.
The effect of carboxylate groups on the complexation of metal ion with oligopeptides – Potentiometric investigation
Abstract Iron(II), iron(III), cobalt(II), zinc(II) cadmium(II) and lead(II) complexes of Asp 2 and Asp 3 and other Asp/Glu containing ligands were studied by potentiometry. Our goal was to study the
...
1
2
3
4
5
...