Evidence map›Paper›PMID 37419072›Full record

ArticleBiosensors & bioelectronics2023

Enzyme - Switch sensors for therapeutic drug monitoring of immunotherapies.

Emma Campbell, Hope Adamson, Declan Kohl, Christian Tiede, Christoph Wälti, Darren C Tomlinson, Lars J C Jeuken

Open access · hybridAbstract read
In one paragraph

Article in Biosensors & bioelectronics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Review
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

7 authors at 2 institutions in 2 countries.

Emma CampbellSchool of Biomedical Science, University of Leeds, Leeds, LS2 9JT, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom.
Hope AdamsonSchool of Biomedical Science, University of Leeds, Leeds, LS2 9JT, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom.
Declan KohlSchool of Biomedical Science, University of Leeds, Leeds, LS2 9JT, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom.
Christian TiedeAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom; School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Christoph WältiSchool of Electronic and Electrical Engineering, University of Leeds, LS2 9JT, United Kingdom.
Darren C TomlinsonAstbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom; School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Lars J C JeukenSchool of Biomedical Science, University of Leeds, Leeds, LS2 9JT, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, United Kingdom; Leiden Institute of Chemistry, Leiden University, PO Box 9502, 2300 RA, Leiden, the Netherlands. Electronic address: L.J.C.Jeuken@lic.leidenuniv.nl.
University of Leeds · GBLeiden University · NL

Funding

Medical Research Council MR/N029976/1Wellcome Trust
6 · The paper itself

Abstract

Therapeutic monoclonal antibodies (TmAb) have emerged as effective treatments for a number of cancers and autoimmune diseases. However, large interpatient disparities in the pharmacokinetics of TmAb treatment requires close therapeutic drug monitoring (TDM) to optimise dosage for individual patients. Here we demonstrate an approach for achieving rapid, sensitive quantification of two monoclonal antibody therapies using a previously described enzyme switch sensor platform. The enzyme switch sensor consists of a β-lactamase - β-lactamase inhibitor protein (BLA-BLIP) complex with two anti-idiotype binding proteins (Affimer proteins) as recognition elements. The BLA-BLIP sensor was engineered to detect two TmAbs (trastuzumab and ipilimumab) by developing constructs incorporating novel synthetic binding reagents to each of these mAbs. Trastuzumab and ipilimumab were successfully monitored with sub nM sensitivity in up to 1% serum, thus covering the relevant therapeutic range. Despite the modular design, the BLA-BLIP sensor was unsuccessful in detecting two further TmAbs (rituximab and adalimumab), an explanation for which was explored. In conclusion, the BLA-BLIP sensors provide a rapid biosensor for TDM of trastuzumab and ipilimumab with the potential to improve therapy. The sensitivity of this platform alongside its rapid action would be suitable for bedside monitoring in a point-of-care (PoC) setting.

Indexed as

Biosensing TechniquesDrug MonitoringAntibodies, MonoclonalHumansImmunotherapyIpilimumabTrastuzumabAntibodies, MonoclonalIpilimumabTrastuzumabAffimer proteinHerceptinHumiraRituxanTherapeutic drug monitoringYervoy

Identifiers

PMID37419072
PMCPMC10427837
OpenAlexW4382812209

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.