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

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,

SUBMITTER: Jia C 

PROVIDER: S-EPMC5643546 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature