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Template‐directed supramolecular assembly of a new type of nanoporous peptide‐based material
Author(s) -
Görbitz Carl Henrik,
Rise Frode
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.985
Subject(s) - stacking , supramolecular chemistry , nanoporous , crystallography , dipeptide , peptide , supramolecular assembly , hexagonal crystal system , materials science , chemistry , self assembly , hydrate , crystal structure , nanotechnology , organic chemistry , biochemistry
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 P 6 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 × 3.5 Å 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. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.