Chiral discrimination in cyclodextrin complexes of amino acid derivatives: β-cyclodextrin/N-acetyl-L-phenylalanine and N-acetyl-D-phenylalanine complexes

Jennifer M. Alexander, Joanna L. Clark, Tom J. Brett, John J. Stezowski

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55 Scopus citations

Abstract

In a systematic study of molecular recognition of amino acid derivatives in solid-state β-cyclodextrin (β-CD) complexes, we have determined crystal structures for complexes of β-cyclodextrin/N-acetyl-L-phenylalanine at 298 and 20 K and for N-acetyl-D-phenylalanine at 298 K. The crystal structures for the N-acetyl-L-phenylalanine complex present disordered inclusion complexes for which the distribution of guest molecules at room temperature is not resolvable; however, they can be located with considerable confidence at low temperature. In contrast, the complex with N-acetyl-D-phenylalanine is well ordered at room temperature. The latter complex presents an example of a complex in this series in which a water molecule is included deeply in the hydrophobic torus of the extended dimer host. In an effort to understand the mechanisms of molecular recognition giving rise to the dramatic differences in crystallographic order in these crystal structures, we have examined the intermolecular interactions in detail and have examined insertion of the enantiomer of the D-complex into the chiral β-CD complex crystal lattice.

Original languageEnglish
Pages (from-to)5115-5120
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number8
DOIs
StatePublished - Apr 16 2002

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