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 - Funding Information:
We thank Prof. Sichun Zhang and Miss Xingyu Si in Tsinghua University for help in HRMS analysis. We are grateful to the financial supports of National Natural Science Foundation of China (21271149 and 21325102), Northwest University (15NW09), and Education Department of Shaanxi (16JS113). The work by R.C. at Oak Ridge National Laboratory (X-ray structural analysis) was supported by the U.S. Department of Energy, Office of Science, Basic Energy Sciences, Chemical Sciences, Geosciences, and Biosciences Division. J.H. and P.H. acknowledge supports from research Project RVO (61388963) of the Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic; Czech Science Foundation (P208/12/G016) and project L01305 of the Ministry of Education, Youth and Sports of the Czech Republic.
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
AN - SCOPUS:85031773590
SN - 2041-1723
VL - 8
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 938
ER -