Evidence map›Paper›PMID 29726557›Full record

ArticleChemical communications (Cambridge, England)2018

Tuning conformation and properties of peptidomimetic backbones through dual N/C

R Kaminker, I Kaminker, W R Gutekunst, Y Luo, S Lee, J Niu, S Han, C J Hawker

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Tuning of protease resistance in oligopeptides through N-alkylation.Chemical communications (Cambridge, England) · 2018
    Article
  5. 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

8 authors.

R KaminkerMaterials Research Laboratory, University of California, Santa Barbara, California 93106, USA. revital@cnsi.ucsb.edu hawker@mrl.ucsb.edu.
I Kaminker
W R Gutekunst
Y Luo
S Lee
J Niu
S Han
C J Hawker

Funding

Development of Sequence Controlled Polymers for Antibacterial Therapeutics and CoF32GM108323 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI GUTEKUNST, WILL RYAN · 2013 to 2015
$143k
NIGMS NIH HHS F32 GM108323
6 · The paper itself

Abstract

We demonstrate that changing the backbone between peptides, peptoids and the underexplored dual N/Cα-substituted peptoids analogues allows for control over the preferred conformation of the intrinsically disordered biomimetic oligomers. The conformation tunability is directly probed using electron paramagnetic resonance (EPR), and is shown to manifest itself in differences in the nanoparticle-oligomer hybridization propensity.

Indexed as

Electron Spin Resonance SpectroscopyNanoparticlesPeptidomimeticsProtein ConformationPeptidomimetics

Identifiers

PMID29726557
PMCPMC6089238

What OpenQuestion holds

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Registered trials

None linked

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.