TY - JOUR
T1 - Selective binding of choline by a phosphate-coordination-based triple helicate featuring an aromatic box
AU - Jia, Chuandong
AU - Zuo, Wei
AU - Yang, Dong
AU - Chen, Yanming
AU - Cao, Liping
AU - Custelcean, Radu
AU - Hostaš, Jiří
AU - Hobza, Pavel
AU - Glaser, Robert
AU - Wang, Yao Yu
AU - Yang, Xiao Juan
AU - Wu, Biao
N1 - Publisher Copyright:
© 2017 The Author(s).
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85031773590&partnerID=8YFLogxK
U2 - 10.1038/s41467-017-00915-8
DO - 10.1038/s41467-017-00915-8
M3 - Article
C2 - 29038482
AN - SCOPUS:85031773590
SN - 2041-1723
VL - 8
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 938
ER -