The influence of penicillamine/cysteine mutation on the metal complexes of peptides
| Autor: | Norbert Lihi, Katalin Várnagy, Ágnes Grenács, Imre Sóvágó |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Circular dichroism Stereochemistry Molecular Conformation chemistry.chemical_element Zinc 010402 general chemistry 01 natural sciences Inorganic Chemistry Metal chemistry.chemical_compound Coordination Complexes Nickel Amide Organic chemistry Amino Acid Sequence Cysteine Peptide sequence chemistry.chemical_classification Cadmium 010405 organic chemistry Circular Dichroism Penicillamine Hydrogen-Ion Concentration 0104 chemical sciences Amino acid chemistry visual_art Potentiometry visual_art.visual_art_medium Peptides |
| Zdroj: | Dalton Trans.. 46:13472-13481 |
| ISSN: | 1477-9234 1477-9226 |
| DOI: | 10.1039/c7dt02703f |
| Popis: | N-Terminally free but C-terminally amidated peptides Pen-SSACS-NH2 and CSSA-Pen-S-NH2 containing l-penicillamine (Pen) in 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 of the synthesis and metal complexes of peptides containing penicillamine in a peptide sequence constructed from natural amino acids. The data were compared to those of the two cysteine counterparts, 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 of the zinc(ii) and cadmium(ii) complexes in the case of all three peptides containing two thiolate functions. |
| Databáze: | OpenAIRE |
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