Evidence map›Paper›PMID 30572602›Full record

ArticleMolecules (Basel, Switzerland)2018

Probing the Structural Determinants of Amino Acid Recognition: X-Ray Studies of Crystalline Ditopic Host-Guest Complexes of the Positively Charged Amino Acids, Arg, Lys, and His with a Cavitand Molecule.

Giovanna Brancatelli, Enrico Dalcanale, Roberta Pinalli, Silvano Geremia

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 31% of its field
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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
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  6. Velcrand Functionalized Polyethylene.Molecules (Basel, Switzerland) · 2019
    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

4 authors at 2 institutions in 1 country.

Giovanna BrancatelliCentre of Excellence in Biocrystallography, Department of Chemical and Pharmaceutical Sciences, University of Trieste, 34127 Trieste, Italy. giovanna_brancatelli@hotmail.com.
Enrico DalcanaleDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, and INSTM, UdR Parma, Parco Area delle Scienze 17/A, 43124 Parma, Italy. enrico.dalcanale@unipr.it.ORCID 0000-0001-6964-788X
Roberta PinalliDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, and INSTM, UdR Parma, Parco Area delle Scienze 17/A, 43124 Parma, Italy. roberta.pinalli@unipr.it.ORCID 0000-0002-0000-8980
Silvano GeremiaCentre of Excellence in Biocrystallography, Department of Chemical and Pharmaceutical Sciences, University of Trieste, 34127 Trieste, Italy. sgeremia@units.it.ORCID 0000-0002-0711-5113
University of Parma · ITUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crystallization of tetraphosphonate cavitand Tiiii[H, CH₃, CH₃] in the presence of positively charged amino acids, namely arginine, lysine, or histidine, afforded host-guest complex structures. The X-ray structure determination revealed that in all three structures, the fully protonated form of the amino acid is ditopically complexed by two tetraphosphonate cavitand molecules. Guanidinium, ammonium, and imidazolium cationic groups of the amino acid side chain are hosted in the cavity of a phosphonate receptor, and are held in place by specific hydrogen bonding interactions with the P=O groups of the cavitand molecule. In all three structures, the positively charged α-ammonium groups form H-bonds with the P=O groups, and with a water molecule hosted in the cavity of a second tetraphosphonate molecule. Furthermore, water-assisted dimerization was observed for the cavitand/histidine ditopic complex. In this 4:2 supramolecular complex, a bridged water molecule is held by two carboxylic acid groups of the dimerized amino acid. The structural information obtained on the geometrical constrains necessary for the possible encapsulation of the amino acids are important for the rational design of devices for analytical and medical applications.

Indexed as

Amino AcidsArginineEthers, CyclicHistidineHydrogen BondingLysineMolecular ConformationResorcinolsAmino AcidsArgininecavitandEthers, CyclicHistidineLysineResorcinolsamino acidargininehistidinehost-guest chemistrylysinemolecular recognitionphosphonate cavitandX-ray structure

Identifiers

PMID30572602
PMCPMC6321202
OpenAlexW2905349308

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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.