Repozytorium
Wyszukaj
Kolekcje
Inne
Influence of the modification of the cosmetic peptide Argireline on the affinity toward copper(II) ions
Autorzy
Rok wydania
2024
Czasopismo
Numer woluminu
30
Strony
e3547/1-e3547/10
DOI
10.1002/psc.3547
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Argireline (Ac-EEMQRR-NH2), a well-known neurotransmitter peptide with a potency similar to botulinum neurotoxins, reveals a proven affinity toward Cu(II) ions. We report herein Cu(II) chelating properties of three new Argireline derivatives, namely, AN4 (Ac-EAHRR-NH2), AN5 (Ac-EEHQRR-NH2), and AN6 (Ac-EAHQRK-NH2). Two complementary experimental techniques, i.e., potentiometric titration (PT) and isothermal titration calorimetry (ITC), have been employed to describe the acid–base properties of the investigated peptides as well as the thermodynamic parameters of the Cu(II) complex formation. Additionally, based on density functional theory (DFT) calculations, we propose the most likely structures of the resulting Cu-peptide complexes. Finally, the cytotoxicity of the free peptides and the corresponding Cu(II) complexes was estimated in human skin cells for their possible future cosmetic application. The biological results were subsequently compared with free Argireline, its Cu(II)-complexes, and the previously studied AN2 derivative (EAHQRR).
Słowa kluczowe
Argireline, complexation process, copper(II) ions, ITC, peptides
Adres publiczny
http://dx.doi.org/10.1002/psc.3547
Strona internetowa wydawcy
Podobne publikacje
Characterization of four peptides from milk fermented with kombucha cultures and their metal complexes—in search of new biotherapeutics
Kamińska Justyna, Hecel Aleksandra, Słowik Joanna, Rombel-Bryzek Agnieszka, Rowińska-Żyrek Magdalena, Witkowska Danuta
The interactions of glycated decapeptide, the Amadori product, with copper(II) ions– a possible effect on the oxidative stress induced aggregation?.
Matera-Witkiewicz Agnieszka, Kapczyńska Katarzyna, Stefanowicz Piotr
Thiol, His–His Motif, and the Battle over Cu(II) in the Relationship of CopM Metallophore and OprC Outer Membrane Protein
Hecel Aleksandra, Kola Arian, Valensin Daniela, Witkowska Danuta