BETA-SHEET PEPTIDE ARCHITECTURE - MEASURING THE RELATIVE STABILITY OF PARALLEL VS ANTIPARALLEL BETA-SHEETS

Nanostructures through self‐assembly: Suitably designed planar cyclic peptides like 1 form cylindrical dimers in nonpolar organic solvents. These ensembles are good models for the fundamental description of parallel and antiparallel β‐sheet structures as well as for the design of novel peptide nanostructures. The analysis of the structural and thermodynamic aspects of the dimerization process showed that the hydrogen bonds between the peptide backbones are crucial factors for the stability of the ensembles and selective formation of β‐sheet arrangements. Furthermore 1 crystallizes to form a novel, porous, solid‐state object with an amphiphilic tubular superlattice, which may have potential utility in the molecular inclusion of hydrophilic and hydrophobic substrates. (Figure Presented.) Copyright © 1995 by VCH Verlagsgesellschaft mbH, Germany