The reaction of histidine‐containing polypeptides with toxic and essential metals and the
molecular mechanism of complexation has yet to be determined, particularly with respect to …

The formation of complexes of HGGGHGHGGGHG (HG12) with copper (II) and nickel (II)
have been studied in aqueous solution under various experimental conditions, including …

The study on the binding ability of tested ligands have shown that insertion of two dehydro-
amino acid residues into peptide sequences makes them more effective in metal ion binding …

Numerous studies have demonstrated the high metal binding capacity and selectivity of
peptide molecules. The terminal amino group, deprotonated amide nitrogens, and various …

Multi-histidinic peptides have been investigated for Cu (II) and Ni (II) binding. We present
spectroscopic evidence that, at low pH and from sub-stoichiometric to stoichiometric …

A novel strategy is presented for designing peptides with specific metal‐ion chelation sites,
based on linking computationally predicted ion‐specific combinations of amino acid side …

The cooperativity of formation of 5-membered and 6-membered chelate rings is the driving
force for specificity and selectivity in Cu (II) peptidic complexes. α-Amino acids enable the …

Copper (II) binary and ternary complexes of dipeptides containing amide carbonyl, alcoholic
hydroxy, and carboxy groups in their side-chain have been studied. The dipeptides (A …

The purpose of our research was to obtain peptidomimetics possessing Cu (II) and Ni (II)
binding properties, which would be useful for biomedical applications. In this context we …

The stoichiometry, stability constants and solution structure of the complexes formed in the
reaction of copper (II) with oligopeptides containing histidyl residues at the C-termini …