Selective Chemical Manipulation of Peptides by Metal Complex Catalysts

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A novel catalysts for chemical modification and/or sequence-specific hydrolysis of peptides were studied.(1) Condensation of glycine with various aldehydes yields β-hydroxyalkyl-substituted glycine, such as serine, threonine, or β-hydroxyphenylalanine. By this study, the followings have been found about this reaction, which open a new way to the chemical modification of peptides and proteins.・ The condensations are remarkably accelerated by multinuclear cupper (II) complexes under mild conditions. The multinuclear complexes work as catalysts resulting a turnover more than unity for the first time.・ An N-terminus glycine residue in oligopeptids is selectively converted into a serine residue by this reaction.・ The trinuclear cupper (II) complex also catalyses oxidative decomposition of amino acids. The trinuclear complex is found to be useful for oxigenation of alkenes under mild conditions.(2) Efficient and sequence-specific hydrolysis of peptides is found to be achieved by cooperation of a metal ion and an internal OH group in the side chain of a peptide. The generality of the specific scission is confirmed by tests using various tripeptides and tetrapeptides.The presence of a histidine residue, which can coordinate metal ion that acts as a catalyst, near the serine residue remarkably enhances the efficiency of the hydrolysis.An alkyl subsitution of the amino acid residue at the N-terminus site of the cleaved peptide bond enhances the rate for the metal-ion-catalysed hydrolysis.