Self-organized supramolecular structures hydrogen-bonding

The rational synthesis of peptide-based nanotubes by self-assembling of polypeptides into a supramolecular structure was demonstrated. This self-organization leads to peptide nanotubes, having channels of 0.8 nm in diameter and a few hundred nanometer long (68). The connectivity of the proteins in these nanotubes is provided by weak bonds, like hydrogen bonds. These structures benefit from the relative flexibility of the protein backbone, which does not exist in nanotubes of covalently bonded inorganic compounds. 

This hydrogen-bond-driven large-scale structural organization has parallels in abiotic systems as well. For example, 1 1 mixtures of ra -l,2-diaminocyclohexane and C2 symmetric 1,2-diols self-assemble into well-defined supramolecular structures which have been characterized by X-ray diffraction analysis. The structures, some of which are stable to sublimation, are helical, the handedness of the helices being determined by the handedness of the 1,2-diamine [222]. 

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