Assembly into β-sheet structures upon peptide-liposome conjugation through copper(I)-catalyzed [3+2] azide-alkyne cycloaddition

The random-coil-to-β-sheet transition of the (Leu-Glu)4 peptide motif is induced upon its conjugation to the liposome surface through "click" chemistry. Circular dichroism (CD) spectroscopy enables the in situ monitoring of this reaction. A change in the peptide secondary structure is already observed within 15 min. The β-sheet conformation becomes the dominant secondary structure after 45 min, as shown by the strong CD signal observed, which is typical for a β-sheet peptide secondary structure. Secondary structures: The random-coil-to-β-sheet transition of the (Leu-Glu)4 peptide motif is induced upon its conjugation to the liposome surface through "click" chemistry (see figure). Circular dichroism (CD) spectroscopy enables the in situ monitoring of this reaction over time. A change in the peptide secondary structure is observed within 15 min, and the β-sheet conformation becomes the dominant secondary structure after 45 min. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.