Molecular selective binding of basic amino acids by a water-soluble pillar[5]arene
Highly selective binding of basic amino acids, i.e. lysine, arginine, and histidine, by a negatively charged carboxylatopillar[5]arene (CP5A) is reported. And the complexation behavior of the CP5A host towards lysine metabolites including cadaverine (Cad), acetyl-l-lysine (AcLys) and trimethyl-l-lys...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2013-01, Vol.49 (19), p.1924-1926 |
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Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Highly selective binding of basic amino acids, i.e. lysine, arginine, and histidine, by a negatively charged carboxylatopillar[5]arene (CP5A) is reported. And the complexation behavior of the CP5A host towards lysine metabolites including cadaverine (Cad), acetyl-l-lysine (AcLys) and trimethyl-l-lysine (TMLys) is also described. |
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ISSN: | 1359-7345 1364-548X |
DOI: | 10.1039/c3cc38622h |