Evidence map›Paper›PMID 40156861›Full record

ArticleNucleic acids research2025

Exploring the relationship between aptamer binding thermodynamics, affinity, and specificity.

Obtin Alkhamis, Caleb Byrd, Juan Canoura, Adara Bacon, Ransom Hill, Yi Xiao

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
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  11. Review
  12. Structural basis and affinity improvement for an ATP-binding DNA aptamer.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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.

Obtin AlkhamisDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.
Caleb ByrdDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.
Juan CanouraDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.
Adara BaconDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.
Ransom HillDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.
Yi XiaoDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, NC 27695, United States.ORCID 0000-0001-7278-9811

Funding

National Institute of Justice, Office of Justice Programs 2022-GG-04440-RESS
6 · The paper itself

Abstract

Aptamers are oligonucleotide-based bioreceptors that are selected in vitro from randomized libraries to bind specific molecules with high affinity, and are proving popular for applications in diagnostics, bioimaging, and therapeutics. A better understanding of aptamer-ligand interactions could facilitate sequence engineering efforts to improve aptamer binding properties, and perhaps eventually allow for the direct design of high-quality aptamers. To date, however, there have been very few comprehensive studies exploring the relationship between aptamer binding properties and thermodynamics. Isothermal titration calorimetry (ITC) is a gold-standard method for studying the thermodynamics of ligand-receptor interactions. In this work, we have compiled ITC-derived thermodynamic binding data from 317 small-molecule-binding DNA aptamers, along with specificity profiles for ∼6000 aptamer-ligand pairs, and performed systematic analysis of the resulting datasets. This analysis revealed a variety of interesting patterns and trends. For example, ligand binding for most aptamers is generally driven solely by enthalpy, and aptamers with the highest binding enthalpy and greatest entropic binding penalties consistently have high specificity. We envision that the expansion and further analysis of such datasets will yield a far better understanding of the complex interplay between the various non-covalent interactions underlying aptamer-ligand recognition.

Indexed as

Aptamers, NucleotideThermodynamicsCalorimetryLigandsAptamers, NucleotideLigands

Identifiers

PMID40156861
PMCPMC11952966

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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.