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

Lesiów, Monika Katarzyna; Bieńko, Alina; Sobańska, Kamila; Kowalik-Jankowska, Teresa; Rolka, Krzysztof; Łęgowska, Anna; Ptaszyńska, Natalia

doi:10.1016/j.jinorgbio.2020.111250

Cited by 8 publications

(8 citation statements)

References 82 publications

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“…The maximum wavelength for the band observed in UV-Vis spectra at 520 nm confirms that the 4N complex is present [ 25 , 26 ]. Moreover, an additional band appears in the CD spectra at 532 nm, suggesting the second amide nitrogen atom in the coordination sphere [ 26 ], which is in a good agreement with data for {2N im , 2N − } obtained for peptides with two His residues (H-X-X-X-H) [ 27 ]. This type of complex could also be confirmed by the absence of the band around 340 nm, which corresponds to the coordination of the His residue in the apical position [ 21 , 28 ].…”

Section: Resultssupporting

confidence: 76%

The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes

Janicka-Kłos

Czapor-Irzabek

Janek

2021

IJMS

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Mucin 7 (encoded byMUC7) is a human salivary protein that has a role in the natural immune system. Fragments of mucin 7 exhibit antimicrobial activity against bacteria and yeast. Although the antimicrobial properties of peptides have been known and studied for decades, the exact mechanism of action of antimicrobial peptides (AMPs) is still unclear. It is known that some AMPs require divalent metal ions to activate their activity. Herein, we investigated three 15-mer MUC7 peptides, one of which (mother peptide, sequence, L3) is a synthetic analog of a fragment naturally excised from MUC7 (with His3, His8, and His 14) and its two structural analogs, containing only two histidine residues, His3, His13 and His8, His13 (L2 and L1, respectively). Since there is a correlation between lipophilicity, the presence of metal ions (such as Cu(II) and Zn(II)) and antimicrobial activity of AMP, antimicrobial properties of the studied peptides, as well as their complexes with Cu(II) and Zn(II) ions, were tested for activity against Gram-positive (Enterococcus faecalis, Staphylococcus epidermidis) and Gram-negative (Escherichia coli, Pseudomonas aeruginosa) bacteria and fungi (Candida albicans). The results were correlated with their lipophilicity. Coordination and thermodynamic studies (potentiometry, UV-Vis, CD) revealed the formation of mainly mononuclear complexes in solution for all studied systems with different stability in the physiological pH range.

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Section: Resultssupporting

confidence: 76%

The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes

Janicka-Kłos

Czapor-Irzabek

Janek

2021

IJMS

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“…35,36 Besides acting as a general base to trigger the hydrolysis reaction, the histidine residue within self-assembling peptides can also coordinate with Cu 2+ ions. 37,38 Molecular interactions between His-containing peptides and Cu 2+ ions were investigated by CD and FTIR spectroscopies. Compared with the CD spectra of self-assembling peptides shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Supramolecular assemblies of histidine-containing peptides with switchable hydrolase and peroxidase activities through Cu(ii) binding and co-assembling

Zhang

Tian

2022

J. Mater. Chem. B

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“…The authors have cited additional references within the Supporting Information. [99][100][101][102][103][104][105][106][107][108][109][110]…”

Section: Supporting Informationmentioning

confidence: 99%

Unravelling the Mystery of COVID‐19 Pathogenesis: Spike Protein and Cu Can Synergize to Trigger ROS Production

Lesiów

Witwicki

Tan

et al. 2023

Chemistry A European J

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The COVID‐19 pandemic has had a devastating impact on global health, highlighting the need to understand how the SARS‐CoV‐2 virus damages the lungs in order to develop effective treatments. Recent research has shown that patients with COVID‐19 experience severe oxidative damage to various biomolecules. We propose that the overproduction of reactive oxygen species (ROS) in SARS‐CoV‐2 infection involves an interaction between copper ions and the virus's spike protein. We tested two peptide fragments, Ac‐ELDKYFKNH‐NH2 (L1) and Ac‐WSHPQFEK‐NH2 (L2), derived from the spike protein of the Wuhan strain and the β variant, respectively, and found that they bind Cu(II) ions and form a three‐nitrogen complexes at lung pH. Our research demonstrates that these complexes trigger the overproduction of ROS, which can break both DNA strands and transform DNA into its linear form. Using A549 cells, we demonstrated that ROS overproduction occurs in the mitochondria, not in the cytoplasm. Our findings highlight the importance of the interaction between copper ions and the virus's spike protein in the development of lung damage and may aid in the development of therapeutic procedures.

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

Cited by 8 publications

References 82 publications

The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes

The Potential Antimicrobial Action of Human Mucin 7 15-Mer Peptide and Its Metal Complexes

Supramolecular assemblies of histidine-containing peptides with switchable hydrolase and peroxidase activities through Cu(ii) binding and co-assembling

Unravelling the Mystery of COVID‐19 Pathogenesis: Spike Protein and Cu Can Synergize to Trigger ROS Production

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