Abstract
Amphiphilic peptide sequences with beta-aminohydroxamic acid (beta ahx) at their C-termini were complexed with Cu2+ ions resulting in formation of stable metallacrowns composed of beta ahx and copper. The ESI-MS data for the obtained compounds show formation of supramolecular structures of M-W approx. 7000 Da with the compositions corresponding to metallacrowns. The addition of Cu2+ to a solution of bahx-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.