Correction: Stability of Cu(II) complexes with FomA protein fragments containing two His residues in the peptide chain.

Correction for 'Stability of Cu(ii) complexes with FomA protein fragments containing two His residues in the peptide chain' by Monika Katarzyna Lesiów et al., Metallomics, 2019, 11, 1518-1531, DOI: 10.1039/C9MT00131J.

Cu(II) complexes with peptides from FomA protein containing -His-Xaa-Yaa-Zaa-His and -His-His-motifs. ROS generation and DNA degradation.

Mono- and dinuclear Cu(II) complexes with Ac-PTVHNEYH-NH (L1) and Ac-NHHTLND-NH (L2) peptides from FomA protein of Fusobacterium nucleatum were studied by potentiometry, spectroscopic methods (UV-Vis, CD, EPR) and MS technique. The dominant mononuclear complexes for L1 ligand are: CuHL (pH range 5.0-6.

Coordination properties of Cu(II) ions towards the peptides based on the His-Xaa-His motif from Fusobacterium nucleatum P1 protein.

The coordination capacity of the copper(II) ions with peptides (fragments of the P1 protein - one of the outer membrane protein from Fusobacterium nucleatum) based on the His-Xaa-His motif was carried out using potentiometric measurements, mass spectrometry and spectroscopic techniques: UV-Vis, CD and EPR. The selected tetrapeptides (Ac-HGHE-NH, Ac-GHEH-NH, Ac-HEHQ-NH and Ac-EHEH-NH) form both mononuclear and bis-complexes with copper(II) ions. In the case of mononuclear complexes the CuL and CuLH species dominate in the solution, where the coordination sphere is create by {2 × N} and {2 × N,2 × N}, respectively.

Copper(ii) complexes with alloferon analogues containing phenylalanine H6F and H12F stability and biological activity lower stabilization of complexes compared to analogues containing tryptophan.

Copper(ii) complex formation processes between alloferon 1 (Allo1) (H1 GVSGH6 GQH9 GVH12G) analogues where the phenylalanine residue is introduced in the place of His residue H6F and H12F have been studied by potentiometric, UV-visible, CD and EPR spectroscopic, and MS methods. For the phenylalanine analogues of alloferon 1, complex speciation has been obtained for a 1 : 1, 2 : 1 and 3 : 1 metal-to-ligand molar ratio. At physiological pH and in 1 : 1 metal-to-ligand molar ratio the phenylalanine analogues of alloferon 1 form a CuL complex similar to that of alanine analogues with the 4N{NH2,N1Im,2NIm} coordination mode.

Stability of Cu(ii) complexes with FomA protein fragments containing two His residues in the peptide chain.

The coordination of Cu(ii) ions by the Ac-KGHGNGEEGTPTVHNE-NH (1L) peptide - a FomA protein fragment of Fusobacterium nucleatum- and its cyclic analogue: cyclo(KGHGNGEEGTPTVHNE) (2L) was studied by potentiometric titration, spectroscopic methods (UV-Vis, CD, EPR) and mass spectrometry (MS). Both the ligands contain two histydyl residues located in the third and fourteenth position of the peptide chain. For the 1L and 2L ligands mono- and dinuclear complexes were identified and studied in an aqueous solution.