Görbitz Carl Henrik
University of Oslo, Department of Chemistry, P.O.Box 1033 Blindern, 0315 Oslo, Norway.
Chemistry. 2007;13(4):1022-31. doi: 10.1002/chem.200601427.
In the last few years dipeptides with two hydrophobic residues (hydrophobic dipeptides) have emerged as an unexpected source of stable microporous organic materials. Supramolecular self-assembly of the rather small building blocks is dictated by stringent demands on the hydrogen-bond formation by the peptide main chains and the aggregation of hydrophobic entities in the side chains. A systematic survey of structures derived from single-crystal X-ray diffraction studies has revealed the existence of two large classes of structures, differing in the dimensionality of the hydrogen-bonding patterns in the crystals and the nature of the channels. The present review summarizes the structural properties of the microporous dipeptides and discusses their potential applications.