Abstract

Abstract Novel helix-peptide wheels, in which three helices were connected by using a template, were prepared, and the dipole–dipole interactions among the helices were studied in relation to the formation of a planar triangle structure containing three helices. The helical segments had a 310-helix structure. 13C spin-lattice relaxation time (T1) measurements showed that the helical segments had restricted mobility. Deuterium exchange rates of amide protons were accelerated in the helix-peptide wheels compared to the respective linear helix peptides, suggesting that there is torsion on the cylindrical shape. Therefore, the predominant structure of the helix-peptide wheels is a planar triangle in solution. Further, the triangle structure was successfully transferred onto a gold substrate.

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