Abstract
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.
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