Confinement of Amino Acids in Tetra-p-Sulfonated Calix[4]arene Bilayers

Jerry L. Atwood, Timothy Ness, Peter J. Nichols, Colin L. Raston

Research output: Contribution to journalArticlepeer-review

100 Citations (Scopus)


Supramolecular complexes of tetra-p-sulfonated calix[4]arene and racemic (alanine, histidine, and phenylalanine) and chiral ((S)-alanine, (S)-histidine, and (S)-tyrosine) amino acids have been isolated in the solid state and their molecular structures elucidated by X-ray diffraction studies. For alanine, histidine, and phenylalanine, racemic pairs of molecules are confined in capsules of tetra-p-sulfonated calix[4]arene in an overall bilayer arrangement. The (S)-amino acid isomers for alanine and histidine, however, formed 1:1 complexes within the bilayer arrangement found for many tetra-p-sulfonated calix[4]arene complexes. For (S)-tyrosine, a π-stacked chiral pair of isomers was encapsulated by tetra-p-sulfonated calix[4]arene.

Original languageEnglish
Pages (from-to)171-176
Number of pages6
JournalCrystal Growth and Design
Issue number3
Publication statusPublished - 1 May 2002
Externally publishedYes


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