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 …

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 …

Previously we demonstrated for several examples that peptides having a general internal
sequence RN-Yaa-Ser/Thr-Xaa-His-Zaa-RC (Yaa= Glu or Ala, Xaa= Ala or His, Zaa= Lys …

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 …

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 …

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 …

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

Previously we demonstrated that Ni (II) complexes of Ac-Thr-Glu-Ser-His-His-Lys-NH2
hexapeptide, representing residues 120-125 of human histone H2A, and some of its …

Selective hydrolysis of peptides promoted by metal ions: a positional scanning approach -
Chemical Communications (RSC Publishing) DOI:10.1039/B202285K Royal Society of …

Creation of synthetic structures with an enzyme-like mechanism and turnover remains a
significant challenge. In this study, peptides containing a cysteine thiol and histidine …