Repozytorium

Asp and His-rich model peptides as a basis for elucidating Mn(II) and Fe(II) peptide coordination chemistry

Autorzy

Karolina Pawlik

Małgorzata Ostrowska

Elżbieta Gumienna-Kontecka

Rok wydania

2026

Czasopismo

Dalton Transactions

Numer woluminu

55

Strony

4664-4676

DOI

10.1039/d6dt00180g

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

Although Mn(II) and Fe(II) ions are essential for all living organisms, particularly pathogenic bacteria, their coordination preferences with peptide ligands remain insufficiently understood. Building on our previous findings and inspired by naturally occurring Mn(II)- and Fe(II)-binding motifs, we designed six model peptides (L1: Ac-HDHDHDHHH-NH2, L2: Ac-HDHDHHHHH-NH2, L3: Ac-HDDHDDHDH-NH2, L4: Ac-HHDDDDHHHH-NH2, L5: Ac-HHDDDHHHH-NH2, and L6: Ac-DDDDDD-NH2) to explore the fundamental aspects of their metal coordination. Spectrometric, spectroscopic (electron paramagnetic resonance), and pH-potentiometric techniques were employed to determine the thermodynamic and structural properties of the resulting complexes. All studied peptides were found to form chelate complexes with Mn(II) and Fe(II) ions, although the stability of the complexes varies. Even though the protonation states of various species differ all investigated complexes remain stable in pH = 7.4. The thermodynamic stability of these complexes is strongly influenced by the peptide architecture, the number and type of potential binding residues, and the overall charge of the system. These findings provide new insights into the coordination behavior of Mn(II) and Fe(II) with histidine- and aspartic acid-rich sequences, contributing to a deeper understanding of metal ion binding in biological systems.

Licencja otwartego dostępu

CC-BY

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Pełny tekst licencji: https://creativecommons.org/licenses/by/3.0/pl/legalcode

Adres publiczny

http://dx.doi.org/10.1039/d6dt00180g

Strona internetowa wydawcy

https://www.rsc.org/

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