Issue 14, 2005

From α-helix to β-sheet – a reversible metal ion induced peptide secondary structure switch

Abstract

Here we introduce a peptide model based on an α-helical coiled coil peptide, providing a simple system which can be used for a systematic study of the impact of different metal ions in different oxidation states on peptide secondary structure on a molecular level; histidine residues were incorporated into the heptad repeat to generate possible complexation sites for Cu2+ and Zn2+ ions.

Graphical abstract: From α-helix to β-sheet – a reversible metal ion induced peptide secondary structure switch

Supplementary files

Article information

Article type
Communication
Submitted
28 Apr 2005
Accepted
25 May 2005
First published
16 Jun 2005

Org. Biomol. Chem., 2005,3, 2500-2502

From α-helix to β-sheet – a reversible metal ion induced peptide secondary structure switch

K. Pagel, T. Vagt, T. Kohajda and B. Koksch, Org. Biomol. Chem., 2005, 3, 2500 DOI: 10.1039/B505979H

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