Journal of Solution Chemistry

, Volume 47, Issue 1, pp 80–91 | Cite as

Investigation of the Binding Properties of the Cosmetic Peptide Argireline and Its Derivatives Towards Copper(II) Ions

  • Joanna MakowskaEmail author
  • Aleksandra Tesmar
  • Dariusz Wyrzykowski
  • Lech Chmurzyński


Isothermal titration calorimetry, potentiometric titration and circular dichroism spectroscopy were used to study the interaction of copper(II) ions with Argireline (Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2) and three of its point mutation derivatives: Glu-Ala-Met-Gln-Arg-Arg-NH2 (AN1), Glu-Ala-His-Gln-Arg-Arg-NH2 (AN2) and Glu-Ala-Met-Gln-Ala-Arg-NH2 (AN3). Under the experimental conditions (20 mmol·L−1 Caco solution, pH 6, 298.15 K), copper(II) ions form 1:1 complexes with the peptides Argireline, AN1, and AN2. The complexation reactions are entropy-driven processes. The stability of the resulting complexes increases in the order log10KCu(AN1) < log10KCu(Argireline) < log10KCu(AN2). The relationship between the point mutations of Argireline and the binding properties of these peptides towards copper(II) ions is discussed.


Argireline ITC Copper(II) ions Complexation process Chemical synthesis CD spectroscopy 


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Authors and Affiliations

  1. 1.Faculty of ChemistryUniversity of GdańskGdańskPoland

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