Potentiometry and UV–vis and circular dichroism spectroscopies were applied to
characterize Cu (II) coordination to the Ac-GASRHWKFL-NH2 peptide. Using HPLC and ESI …

Previously we demonstrated the sequence-specific hydrolysis of the R1-(Ser/Thr)-peptide
bond in Ni (II) complexes of peptides with a general R1-(Ser/Thr)-Xaa-His-Zaa-R2 sequence …

Complex formation of the copper (II) ion (CuII) with histidine (H) and H-containing peptides
plays a crucial role in various metallo-enzymatic reactions. To elucidate the nature of …

A combined pH-metric and spectroscopic (UV—Vis, circular dichroism and electron
paramagnetic resonance) study of Cu (II) binding to analogues of Asn-Ser-Phe-Arg-Tyr-NH2 …

The observed variety of metal-ion complexation sites offered by peptides reflects a basic
tension between charge solvation of the ion by Lewis-basic chelating groups versus amide …

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 …

The hydrolysis of glycylglycine (GylGly), glycyl-L-leucine (GlyLeu), L-leucylglycine (LeuGly)
and glycyl-DL-serine (GlySer) promoted by a copper (II)-cis, cis-1, 3, 5-triaminocyclohexane …

Protonation of copper (II)-and nickel (II) tetrapeptide complexes with bulky α-carbon
substituents has been studied. The pK a-values for the second and terminal metal–N …

Copper (III) complexes of Gly2HisGly and Aib2HisGly are characterized, where Gly is
glycine, His is l-histidine, and Aib is α-aminoisobutyric acid. Their respective reduction …

Five peptides containing (His‐X2)‐His or (His‐X3)‐His motifs have been designed and
synthesized to coordinate Cu (II). Structural information was obtained by various …