6533b82cfe1ef96bd128ec5c

RESEARCH PRODUCT

Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus

Kinga GarstkaAleksandra HecelHenryk KozłowskiMagdalena Rowińska-żyrek

subject

Binding SitesAspergillus fumigatusZn(II)- and Ni(II)-binding peptidesMetals and AlloysBiophysicsBiochemistryBiomaterialsZincthermodynamicsProtein DomainsChemistry (miscellaneous)zincophorepotentiometryHumansAmino Acids

description

Abstract Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. In this work, we focus on the thermodynamics of Zn(II) complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, we show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni(II) does not compete with Zn(II) binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn(II) via two Cys thiolates and two His imidazoles and it could be considered as a promising A. fumigatus targeting molecule.

yearjournalcountryeditionlanguage
2022-01-28Metallomics
10.1093/mtomcs/mfac042https://academic.oup.com/metallomics/article/14/7/mfac042/6608364