Microporous organic materials from hydrophobic dipeptides.
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.
Görbitz
Carl Henrik
CH
University of Oslo, Department of Chemistry, P.O.Box 1033 Blindern, 0315 Oslo, Norway. c.h.gorbitz@kjemi.uio.no
D004151:Dipeptides / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D016062:Porosity; D011487:Protein Conformation
D004151:Dipeptides