Document Detail


Molecular selective binding of basic amino acids by a water-soluble pillar[5]arene.
MedLine Citation:
PMID:  23361588     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Chunju Li; Junwei Ma; Liu Zhao; Yanyan Zhang; Yihua Yu; Xiaoyan Shu; Jian Li; Xueshun Jia
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-29
Journal Detail:
Title:  Chemical communications (Cambridge, England)     Volume:  -     ISSN:  1364-548X     ISO Abbreviation:  Chem. Commun. (Camb.)     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9610838     Medline TA:  Chem Commun (Camb)     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Chemistry, Shanghai University, Shanghai 200444, P. R. China. cjli@shu.edu.cn xsjia@mail.shu.edu.cn.
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