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-lysine (TMLys) is also described.
Department of Chemistry, Shanghai University, Shanghai 200444, P. R. China. cjli@shu.edu.cn
Chunju
C
Li
Junwei
J
Ma
Liu
L
Zhao
Yanyan
Y
Zhang
Yihua
Y
Yu
Xiaoyan
X
Shu
Jian
J
Li
Xueshun
X
Jia
D024361:Amino Acids, Basic / Q000737:chemistry*; D047250:Calixarenes; D000644:Quaternary Ammonium Compounds / Q000737:chemistry*; D012995:Solubility; D013379:Substrate Specificity; D014867:Water / Q000737:chemistry*
D024361:Amino Acids, Basic; D000644:Quaternary Ammonium Compounds; C570642:pillar(5)arene; D014867:Water; D047250:Calixarenes