Evidence map›Paper›PMID 38873052›Full record

ArticleChemical science2024

Site-directed conjugation of single-stranded DNA to affinity proteins: quantifying the importance of conjugation strategy.

Andres Rocha Tapia, Fabrice Abgottspon, Johan Nilvebrant, Per-Åke Nygren, Sarah Duclos Ivetich, Andres Javier Bello Hernandez, Ioanna A Thanasi, Peter A Szijj, Ghali Sekkat, François M Cuenot and 4 more

Abstract read
In one paragraph

Article in Chemical science, 2024. 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.

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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

14 authors.

Andres Rocha TapiaInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.ORCID https://orcid.org/0000-0001-7236-6042
Fabrice AbgottsponInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.
Johan NilvebrantDepartment of Protein Science, KTH Royal Institute of Technology, AlbaNova University Center 106 91 Stockholm Sweden.ORCID https://orcid.org/0000-0002-6104-6446
Per-Åke NygrenDepartment of Protein Science, KTH Royal Institute of Technology, AlbaNova University Center 106 91 Stockholm Sweden.
Sarah Duclos IvetichInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.
Andres Javier Bello HernandezInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.
Ioanna A ThanasiDepartment of Chemistry, University College London 20 Gordon Street WC1H 0AJ London UK.
Peter A SzijjDepartment of Chemistry, University College London 20 Gordon Street WC1H 0AJ London UK.ORCID https://orcid.org/0000-0002-2944-2676
Ghali SekkatInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.
François M CuenotDepartment of Biology, Institute of Molecular Health Sciences, ETH Zurich Otto-Stern-Weg 7 8093 Zürich Switzerland.ORCID https://orcid.org/0009-0005-4028-8955
Vijay ChudasamaDepartment of Chemistry, University College London 20 Gordon Street WC1H 0AJ London UK.ORCID https://orcid.org/0000-0002-8876-3285
Nicola AcetoDepartment of Biology, Institute of Molecular Health Sciences, ETH Zurich Otto-Stern-Weg 7 8093 Zürich Switzerland.
Andrew J deMelloInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.ORCID https://orcid.org/0000-0003-1943-1356
Daniel A RichardsInstitute for Chemical and Bioengineering, ETH Zurich Vladimir-Prelog-Weg 1 8093 Zürich Switzerland daniel.richards@chem.ethz.ch.ORCID https://orcid.org/0000-0001-8827-9170

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Affinity protein-oligonucleotide conjugates are increasingly being explored as diagnostic and therapeutic tools. Despite growing interest, these probes are typically constructed using outdated, non-selective chemistries, and little has been done to investigate how conjugation to oligonucleotides influences the function of affinity proteins. Herein, we report a novel site-selective conjugation method for furnishing affinity protein-oligonucleotide conjugates in a 93% yield within fifteen minutes. Using SPR, we explore how the choice of affinity protein, conjugation strategy, and DNA length impact target binding and reveal the deleterious effects of non-specific conjugation methods. Furthermore, we show that these adverse effects can be minimised by employing our site-selective conjugation strategy, leading to improved performance in an immuno-PCR assay. Finally, we investigate the interactions between affinity protein-oligonucleotide conjugates and live cells, demonstrating the benefits of site-selective conjugation. This work provides critical insight into the importance of conjugation strategy when constructing affinity protein-oligonucleotide conjugates.

Identifiers

PMID38873052
PMCPMC11168188

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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.