Influence of amino acids sequence on metal binding properties of selected pentapeptides - fluorescence and UV-Vis spectroscopy studies

Interactions between peptides and metal ions are the subject of constant investigations, as they are considered to be of great significance. For instance, it has been shown that several ions, e.g. Cu2+ and Zn2+, are involved in the amyloid-β peptide aggregation process, which presumably plays the main role in Alzheimer’s disease (Nair, Perry, Smith, & Reddy, 2010). From among all amino acids present in the Aβ sequence, histidine and tyrosine side chains are proven to have a distinct affinity for Cu2+ and other metal cations (Murariu et al., 2018). The aim of our work was to investigate potential applications of fluorescence and UV-Vis spectroscopy for research into interactions between several metal cations (Mn2+, Fe2+, Co2+, Ni2+, Cu2+ and Zn2+) and four selected peptides (EYHHQ, EHYHQ, EHHQY and KYHHE).