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.
Chemical Communications
- Information Point