In our previous research we demonstrated the sequence specific peptide bond hydrolysis of
the R 1-(Ser/Thr)-Xaa-His-Zaa-R 2 in the presence of Ni (II) ions. The molecular mechanism …

Recently, we described a sequence-specific R1-(Ser/Thr) peptide bond hydrolysis reaction
in peptides of a general sequence R1–(Ser/Thr)–Xaa–His–Zaa–R, which occurs in the …

In previous studies we showed that Ni (II) ions can hydrolytically cleave a peptide bond
preceding Ser/Thr in peptides of a general sequence RN–(Ser/Thr)–Xaa–His–Zaa–RC …

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 …

Metal-assisted hydrolysis of peptide bond is a promising alternative for enzymatic cleavage
of proteins with prospective applications in biochemistry and bioengineering. Many metal …

Recently we screened a combinatorial library of R1-(Ser/Thr)-Xaa-His-Zaa-R2 peptides
(Xaa= 17 common α-amino acids, except Asp, Glu, and Cys; Zaa= 19 common α-amino …

Hydrolysis of amide bonds by metal complexes has been of great interest since it was
revealed that the active site of carboxypeptidase A contains a zinc ion [1]. The task of …

Copper–peptide complexes have been the most extensively studied of all the metal–peptide
complexes. Copper (II) is the most important oxidation state in copper–peptide complexes …

Metal ions and complexes that hydrolyze peptides under nondenaturing conditions of
temperature and pH hold great promise for use in protein structural studies. However, the …

Several reports have highlighted the interest of replacing Gly, a frequent amino acid within
bioactive peptides, by azaGly (Agly) to improve their stability, activity or for the design of …