Wydział Chemii

Silvia Leveraro

Valentyn Dzyhovskyi

Kinga Garstka

Agnieszka Szebesczyk

Fabio Zobi

Denise Bellotti

Kamila Stokowa-Sołtys

Maurizio Remelli

Magdalena Rowińska-Żyrek

2025

Inorganic Chemistry

64

6751-6760

10.1021/acs.inorgchem.5c00672

Naukowa

Angielski

Artykuł

Amide groups of the peptide backbone are very weak acids. In fact, their deprotonation in water solution is not a phenomenon usually observed in the measuring range of a glass electrode unless the proton is displaced by a metal such as Cu(II) or Ni(II). Other metals are not usually expected to deprotonate and bind to amide nitrogens, although, lately, some controversies have started to arise in the literature, suggesting that Zn(II) and Fe(II) may be capable of doing so. In order to clarify this phenomenon, we chose to study simple metal–peptide systems with Ala-to-Pro mutations, which excluded further amides from binding. A comparison of the metal-binding modes of Ac-AAAHAAA-NH₂, Ac-AAPHAAA-NH₂, and Ac-AAPHPAA-NH₂ complexes with Cu(II), Zn(II), and Fe(II) is a simple and elegant way of showing that neither Zn(II) nor Fe(II) is able to deprotonate and bind to amide nitrogens.

Amides, Ions, Metals, Nitrogen, Peptides and proteins

CC-BY

http://dx.doi.org/10.1021/acs.inorgchem.5c00672

https://www.acs.org/content/acs/en.html