Folding a De Novo Designed Peptide into an α‐Helix through Hydrophobic Binding by a Bowl‐Shaped Host

In a twist: Encapsulation of a nine-residue peptide (Trp-Ala-Glu-Ala-Ala-Ala-Glu-Ala-Trp) within a bowl-shaped coordination host in water induces and stabilizes the α-helical conformation. The α-helical peptide is recognized through two types of host–guest interactions: a hydrophobic interaction with both terminal Trp residues and electrostatic interactions between the Glu residues and the high positive charge of the host (12+). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2006/z502802_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.