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The influence of penicillamine/cysteine mutation on the metal complexes of peptides

Abstract

The N-terminally free but C-terminally amidated peptides Pen-SSACS-NH2 and CSSA-Pen-S-NH2 containing L-penicillamine (Pen) in the sequence have been synthesized and their nickel(II), zinc(II) and cadmium(II) complexes were studied by potentiometric and spectroscopic measurements. This study is the first example for the synthesis and metal complexes of peptides containing penicillamine in a peptide sequence built up from natural amino acids. The data were compared to those of the two cysteine counterpart CSSACS-NH2. It was found that the replacement of L-cysteine with L-penicillamine has a significant impact on the complex formation processes with nickel(II) ions. The major differences include the suppression of polynuclear complex formation, the enhanced metal binding affinity of the amino terminus and the increased tendency for the formation of amide bonded species. The tridentate (NH2,S–,S–) coordination was characteristic for the zinc(II) and cadmium(II) complexes in the case of all three peptides containing two thiolate functions.

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Publication details

The article was received on 24 Jul 2017, accepted on 12 Sep 2017 and first published on 12 Sep 2017


Article type: Paper
DOI: 10.1039/C7DT02703F
Citation: Dalton Trans., 2017, Accepted Manuscript
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    The influence of penicillamine/cysteine mutation on the metal complexes of peptides

    Á. Grenács, N. Lihi, I. Sóvágó and K. Várnagy, Dalton Trans., 2017, Accepted Manuscript , DOI: 10.1039/C7DT02703F

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