Evidence map›Paper›PMID 34659704›Full record

ArticleChemical science2021

RE-SELEX: restriction enzyme-based evolution of structure-switching aptamer biosensors.

Aimee A Sanford, Alexandra E Rangel, Trevor A Feagin, Robert G Lowery, Hector S Argueta-Gonzalez, Jennifer M Heemstra

Abstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Review
  6. Article
  7. START: A Versatile Platform for Bacterial Ligand Sensing with Programmable Performances.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Rationally Designed DNA-Based Scaffolds and Switching Probes for Protein Sensing.Advances in biochemical engineering/biotechnology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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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.

Aimee A SanfordDepartment of Chemistry, Emory University Atlanta Georgia 30322 USA jen.heemstra@emory.edu.ORCID https://orcid.org/0000-0001-5170-943X
Alexandra E RangelDepartment of Chemistry, Center for Cell and Genome Science, University of Utah Salt Lake City Utah 84112 USA.
Trevor A FeaginDepartment of Chemistry, Center for Cell and Genome Science, University of Utah Salt Lake City Utah 84112 USA.
Robert G LoweryBellBrook Labs, LLC Madison Wisconsin 53711 USA.
Hector S Argueta-GonzalezDepartment of Chemistry, Emory University Atlanta Georgia 30322 USA jen.heemstra@emory.edu.
Jennifer M HeemstraDepartment of Chemistry, Emory University Atlanta Georgia 30322 USA jen.heemstra@emory.edu.ORCID https://orcid.org/0000-0002-7691-8526

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aptamers are widely employed as recognition elements in small molecule biosensors due to their ability to recognize small molecule targets with high affinity and selectivity. Structure-switching aptamers are particularly promising for biosensing applications because target-induced conformational change can be directly linked to a functional output. However, traditional evolution methods do not select for the significant conformational change needed to create structure-switching biosensors. Modified selection methods have been described to select for structure-switching architectures, but these remain limited by the need for immobilization. Herein we describe the first homogenous, structure-switching aptamer selection that directly reports on biosensor capacity for the target. We exploit the activity of restriction enzymes to isolate aptamer candidates that undergo target-induced displacement of a short complementary strand. As an initial demonstration of the utility of this approach, we performed selection against kanamycin A. Four enriched candidate sequences were successfully characterized as structure-switching biosensors for detection of kanamycin A. Optimization of biosensor conditions afforded facile detection of kanamycin A (90 μM to 10 mM) with high selectivity over three other aminoglycosides. This research demonstrates a general method to directly select for structure-switching biosensors and can be applied to a broad range of small-molecule targets.

Identifiers

PMID34659704
PMCPMC8442683

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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.