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

Metal ions and complexes that hydrolyze peptides and proteins have become increasingly
important in recent years. These reagents have shown great promise for use in a variety of …

Catalysis by metal ions in organic reactions is classified into three categories: Lewis acid
catalysis, catalysis via redox reactions, and catalysis via organometallic compounds (1) …

Artificial peptidases are valuable tools for future biotechnology, and their preparation has
constituted a highly challenging task for chemists. If naturally occurring proteins can be cut at …

Hydrolytic reactions between cis-[Pd (l-Ala-N, O) Cl2]− and cis-[Pd (l-Ala-N, O)(H2O) 2]+, in
which l-Ala is alanine coordinated through N and O atoms, and N-acetylated peptides l …

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 …

Dipeptides having a serine residue at the C-terminus, X-Ser, where X is an appropriate
amino acid residue, were efficiently hydrolyzed in the presence of ZnCl2 at pH 7.0. The rapid …

This seems to be the first report that a transition-metal complex bonded to a histidine residue
effects hydrolytic cleavage of a peptide next to this residue. Dipeptides AcHis-Aa in which …

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 …