Evidence map›Paper›PMID 29038482›Full record

ArticleNature communications2017

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 and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Helical Anion Foldamers in Solution.Chemical reviews · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Chuandong JiaKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Wei ZuoKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Dong YangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Yanming ChenKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Liping CaoKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Radu CustelceanChemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831-6119, USA.
Jiří HostašInstitute of Organic Chemistry and Biochemistry, 16010, Prague 6, Czech Republic.
Pavel HobzaInstitute of Organic Chemistry and Biochemistry, 16010, Prague 6, Czech Republic.
Robert GlaserDepartment of Chemistry, Ben-Gurion University of the Negev, 84105, Beer-Sheva, Israel.
Yao-Yu WangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Xiao-Juan YangKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China.
Biao WuKey Laboratory of Synthetic and Natural Functional Molecule Chemistry of the Ministry of Education, College of Chemistry and Materials Science, Northwest University, 710069, Xi'an, China. wubiao@nwu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.The choline-binding protein ChoX exhibits a synergistic dual-site binding mode that allows it to discriminate choline over structural analogues. Here, the authors design a biomimetic triple anion helicate receptor whose selectivity for choline arises from a similar binding mechanism.

Indexed as

Protein DomainsAcetylcholineBacterial ProteinsBinding, CompetitiveBinding SitesCarrier ProteinsCholineCrystallography, X-RayKineticsMembrane Transport ProteinsModels, MolecularPhosphatesProtein BindingProton Magnetic Resonance SpectroscopySinorhizobium melilotiAcetylcholineBacterial ProteinsCarrier ProteinsCholinecholine transporterMembrane Transport ProteinsPhosphates

Identifiers

PMID29038482
PMCPMC5643546

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.