Wydział Chemii

Dorota Dudek

Adriana Miller

Aleksandra Hecel

Arian Kola

Daniela Valensin

Aleksandra Mikołajczyk

Miquel Barceló-Oliver

Agnieszka Matera-Witkiewicz

Magdalena Rowińska-Żyrek

2023

Inorganic Chemistry

62

14103-14115

10.1021/acs.inorgchem.3c02390

Naukowa

Angielski

Artykuł

Proteolytic degradation of semenogelins, the most abundant proteins from human semen, results in the formation of 26- and 29-amino acid peptides (SgIIA and SgI-29, respectively), which share a common 15 amino acid fragment (Sg-15). All three ligands are effective Zn(II) and Cu(II) binders; in solution, a variety of differently metalated species exist in equilibrium, with the [NH₂, 3N_im] donor set prevailing at physiological pH in the case of both metals. For the first time, the Cu(II)-induced antimicrobial activity of Sg-15 against Enterococcus faecalis is shown. In the case of the two native semenogelin fragment metal complexes, the strong local positive charge in the metal-bound HH motif correlates well with their antimicrobial activity. A careful analysis of semenogelins’ metal coordination behavior reveals two facts: (i) The histamine-like Cu(II) binding mode of SgI-29 strongly increases the stability of such a complex below pH 6 (with respect to the non-histamine-like binding of SgIIA), while in the case of the SgI-29 Zn(II)-histamine-like species, the stability enhancement is less pronounced. (ii) The HH sequence is a more tempting site for Cu(II) ions than the HXH one.

Amines, Imidazoles, Ions, Monomers, Peptides and proteins

CC-BY

http://dx.doi.org/10.1021/acs.inorgchem.3c02390

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