Amide bonds are the most prevalent structures found in organic molecules and various
biomolecules such as peptides, proteins, DNA, and RNA. The unique feature of amide …

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

A recent study [Angew. Chem. Int. Ed. 2015, 54, 7391–7394] has shown that horse heart
myoglobin (HHM) is selectively hydrolyzed by a range of zirconium (IV)‐substituted …

It was previously reported that D‐amino acid‐containing peptides exhibited the ability to
resist enzymatic hydrolysis. This study investigated the influence of mini‐PEGs modification …

The isomerization of l-amino acids in peptides and proteins into d-configuration under
physiological conditions would affect the physiological dysfunction and caused protein …

Abstract A decapeptide, DEHGTAVMLK (DP1), and its random scrambled version,
THMVLAKGED (DP2), have been studied for their interactions with manganese. The amino …

Nickel is harmful for humans, but molecular mechanisms of its toxicity are far from being fully
elucidated. One of such mechanisms may be associated with the Ni (II)-dependent peptide …

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 …

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 …

In this work we demonstrate that the previously described reaction of sequence specific Ni
(ii)-dependent hydrolytic peptide bond cleavage can be performed in complex …