Key points are not available for this paper at this time.
Highly selective binding of basic amino acids, i.e. lysine, arginine, and histidine, by a negatively charged carboxylatopillar5arene (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.
Li et al. (Tue,) studied this question.