期刊
CHEMICAL COMMUNICATIONS
卷 49, 期 19, 页码 1924-1926出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3cc38622h
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资金
- NNSFC [21272155, 21272147, 20902057]
- Shanghai Municipal Education Commission [13YZ010]
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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