title: Template-directed supramolecular assembly of a new type of nanoporous peptide-based material.
abstract: Dipeptides with two hydrophobic residues are known to often form crystals with hydrophobic or hydrophilic channels. One of the exceptions is Leu-Ile, which has been previously shown to crystallize as a nonporous 0.75 hydrate in the hexagonal space group P6(1) with Z' = 4. We have now found that in the presence of D-Leu, a second pseudopolymorph of the dipeptide is formed. The crystal structure has hydrophilic, water-filled channels with an irregular cross section of approximately 5.5 x 3.5 A and constitutes the first example of a crystal packing arrangement where the direction of the channels is perpendicular to the direction of hydrophobic stacking of side chains rather than parallel as in all other porous peptide-based materials.
authors.affiliation: Department of Chemistry, University of Oslo, Blindern, N-0315 OSLO, Norway. c.h.gorbitz@kjemi.uio.no
authors.forename: Carl Henrik
authors.initials: CH
authors.lastname: Görbitz
authors.forename: Frode
authors.initials: F
authors.lastname: Rise
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D016062:Porosity
chemical_list: D010455:Peptides