Evidence map›Paper›PMID 31599485›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

A Chemical Biology Approach to Understanding Molecular Recognition of Lipid II by Nisin(1-12): Synthesis and NMR Ensemble Analysis of Nisin(1-12) and Analogues.

Rachael Dickman, Emma Danelius, Serena A Mitchell, D Flemming Hansen, Máté Erdélyi, Alethea B Tabor

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Ensemble determination by NMR data deconvolution.Nature reviews. Chemistry · 2023
    Review
  5. Going Viral: An Investigation into the Chameleonic Behaviour of Antiviral Compounds.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

6 authors.

Rachael DickmanDepartment of Chemistry, University College London, 20, Gordon Street, London, WC1H 0AJ, UK.ORCID http://orcid.org/0000-0003-3139-5423
Emma DaneliusThe Swedish NMR Centre, Medicinaregatan 5, 40530, Gothenburg, Sweden.ORCID http://orcid.org/0000-0002-7322-9661
Serena A MitchellDepartment of Chemistry, University College London, 20, Gordon Street, London, WC1H 0AJ, UK.
D Flemming HansenInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London, WC1E 6BT, UK.ORCID http://orcid.org/0000-0003-0891-220X
Máté ErdélyiThe Swedish NMR Centre, Medicinaregatan 5, 40530, Gothenburg, Sweden.ORCID http://orcid.org/0000-0003-0359-5970
Alethea B TaborDepartment of Chemistry, University College London, 20, Gordon Street, London, WC1H 0AJ, UK.ORCID http://orcid.org/0000-0001-8216-0347

Funding

Biotechnology and Biological Sciences Research Council BB/R000255/1Engineering and Physical Sciences Research Council EP/L504889/1Engineering and Physical Sciences Research Council EP/N509577/1Vetenskapsrådet 2016:03602Wellcome TrustWellcome Trust 101569/z/13/z
6 · The paper itself

Abstract

Natural products that target lipid II, such as the lantibiotic nisin, are strategically important in the development of new antibacterial agents to combat the rise of antimicrobial resistance. Understanding the structural factors that govern the highly selective molecular recognition of lipid II by the N-terminal region of nisin, nisin(1-12), is a crucial step in exploiting the potential of such compounds. In order to elucidate the relationships between amino acid sequence and conformation of this bicyclic peptide fragment, we have used solid-phase peptide synthesis to prepare two novel analogues of nisin(1-12) in which the dehydro residues have been replaced. We have carried out an NMR ensemble analysis of one of these analogues and of the wild-type nisin(1-12) peptide in order to compare the conformations of these two bicyclic peptides. Our analysis has shown the effects of residue mutation on ring conformation. We have also demonstrated that the individual rings of nisin(1-12) are pre-organised to an extent for binding to the pyrophosphate group of lipid II, with a high degree of flexibility exhibited in the central amide bond joining the two rings.

Indexed as

Amino Acid SequenceHydrogen BondingNisinNuclear Magnetic Resonance, BiomolecularPeptidesProtein ConformationUridine Diphosphate N-Acetylmuramic Acidmuramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenolNisinPeptidesUridine Diphosphate N-Acetylmuramic Acidantibioticscyclic peptideslantibioticsNMR spectroscopysolid phase synthesis

Identifiers

PMID31599485
PMCPMC6899958

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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.