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- W2761310592 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." @default.
- W2761310592 created "2017-10-20" @default.
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- W2761310592 date "2017-10-16" @default.
- W2761310592 modified "2023-10-01" @default.
- W2761310592 title "Selective binding of choline by a phosphate-coordination-based triple helicate featuring an aromatic box" @default.
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- W2761310592 doi "https://doi.org/10.1038/s41467-017-00915-8" @default.
- W2761310592 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5643546" @default.
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