Amphiphilic peptide sequences with β-aminohydroxamic acid (βahx) at their C-termini were complexed with Cu2+ ions resulting in formation of stable metallacrowns composed of βahx and copper. The ESI-MS data for the obtained compounds show formation of supramolecular structures of MW approx. 7000 Da with the compositions corresponding to metallacrowns. The addition of Cu2+ to a solution of βahx-containing peptides results in distinct changes in the CD spectra indicating a shift of their conformational equilibria toward helical structures. The experiments with enzymatic hydrolysis show that formation of metallacrown systems significantly increases the proteolytic stability of investigated peptides.
ASJC Scopus subject areas
- Materials Chemistry