Coordination pattern and reactivity of two model peptides from porin protein P1

• Published in: Journal of inorganic biochemistry 2021-02, Vol.215, p.111332-111332, Article 111332
• Main Authors: Stokowa-Sołtys, Kamila, Dzyhovskyi, Valentyn, Wieczorek, Robert, Jeżowska-Bojczuk, Małgorzata
• Format: Article
• Language: English
• Subjects: Copper(II) coordination; DNA degradation; Fenton-like reaction; Fusobacterium nucleatum; Porin protein P1; Pro-oxidant
• ISSN: 0162-0134; 1873-3344
• DOI: 10.1016/j.jinorgbio.2020.111332

It has been reported that numerous of Fusobacterium nucleatum outer membrane proteins take part in cancerogenesis. Therefore, it is very interesting to study their interactions with metal ions and the ability to produce reactive oxygen species, which may be involved in cancer progression. Since investigations of metal binding to proteins are often based on fragments that contain the metal-binding domains, designing model peptides should be very mindful. As was shown in this paper, very similar protein fragments may behave differentially. Herein, combined potentiometric, spectroscopic, and computational studies were performed to determine metal ion binding by ligands constituting fragments of porin protein P1. Two studied tetrapeptides (Ac–KEHK–NH2 and Ac–EHKA–NH2) that have common EHK motif have different coordination properties and reactivity. Therefore, we should be cautious when transferring the behavior of small peptide fragments to whole protein. [Display omitted] •Model peptides in coordination partial studies of full-length proteins.•DFT methods in prediction of structure and stability of the metal-peptide complexes.•Metal ion complexes with histidine-containing peptides.•Thermodynamic and spectroscopic studies of porin protein fragments from F. nucleatum.•Copper(II) complexes cleave DNA in the presence of H2O2 or ascorbic acid.