Use of diethanolammonium–tetrachloridopalladate(II) complex in bioorganic modelling as artificial metallopeptidase in the reaction with N-acetylated L-methionylglycine dipeptide. NMR and DFT study of the hydrolytic reaction

Hydrolytic activity of diethanolammonium–tetrachloridopalladate(II) complex was tested in the reaction with AcMet-Gly at pH = 2.0 and 60 °C. The reaction was monitored using 1H NMR spectroscopy, during the course of 45 h. It was shown that regioselective cleavage of amide bond involving the carboxylic group of methionine is achieved under these experimental conditions. DFT study was performed, in order to explore the mechanism of this hydrolytic reaction. This study contributes to a better understanding of the mechanism of the peptide bond hydrolysis of the methionine-containing peptides, and generally interaction of Pd(II) with –SR groups of biological relevant molecules.