Selective binding of choline by a phosphate-coordination-based triple helicate featuring an aromatic box

Chuandong Jia, Wei Zuo, Dong Yang, Yanming Chen, Liping Cao, Radu Custelcean, Jiří Hostaš, Pavel Hobza, Robert Glaser, Yao-Yu Wang, Xiao-Juan Yang and Biao Wu ()
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Chuandong Jia: Northwest University
Wei Zuo: Northwest University
Dong Yang: Northwest University
Yanming Chen: Northwest University
Liping Cao: Northwest University
Radu Custelcean: Oak Ridge National Laboratory
Jiří Hostaš: Institute of Organic Chemistry and Biochemistry
Pavel Hobza: Institute of Organic Chemistry and Biochemistry
Robert Glaser: Ben-Gurion University of the Negev
Yao-Yu Wang: Northwest University
Xiao-Juan Yang: Northwest University
Biao Wu: Northwest University

Nature Communications, 2017, vol. 8, issue 1, 1-8

Abstract: Abstract In nature, proteins have evolved sophisticated cavities tailored for capturing target guests selectively among competitors of similar size, shape, and charge. The fundamental principles guiding the molecular recognition, such as self-assembly and complementarity, have inspired the development of biomimetic receptors. In the current work, we report a self-assembled triple anion helicate (host 2) featuring a cavity resembling that of the choline-binding protein ChoX, as revealed by crystal and density functional theory (DFT)-optimized structures, which binds choline in a unique dual-site-binding mode. This similarity in structure leads to a similarly high selectivity of host 2 for choline over its derivatives, as demonstrated by the NMR and fluorescence competition experiments. Furthermore, host 2 is able to act as a fluorescence displacement sensor for discriminating choline, acetylcholine, l-carnitine, and glycine betaine effectively.

Date: 2017
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DOI: 10.1038/s41467-017-00915-8

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