Evidence map›Paper›PMID 41989091›Full record

ArticleProtein engineering, design & selection : PEDS2026

Engineering affibody domains as anti-idiotypic masks for nivolumab-based prodrugs.

Anna Mestre Borras, Hanna Mehari, Stefan Ståhl, John Löfblom

Abstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2026. 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
–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

1 citing paper in PubMed.

  1. Imaging of ROR1 expression in tumors using radiolabeled affibody molecules.European journal of nuclear medicine and molecular imaging · 2026
    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

4 authors.

Anna Mestre BorrasDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-106 91, Stockholm, Sweden.ORCID 0000-0001-5365-9122
Hanna MehariDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-106 91, Stockholm, Sweden.ORCID 0009-0002-3941-1600
Stefan StåhlDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-106 91, Stockholm, Sweden.
John LöfblomDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, SE-106 91, Stockholm, Sweden.ORCID 0000-0001-9423-0541

Funding

CellNova center 2017/02105, JLHjärnfonden FO2022-0253Hjärnfonden FO2023-0141, JLKnut and Alice Wallenberg Foundation KAW 2023.0073Knut and Alice Wallenberg Foundation KAW 2023.0512Swedish Agency for Innovation VINNOVA 2019/00104Swedish Cancer Society 20 1090 PjF; JLSwedish Cancer Society CAN 23 2717 Pj; JLSwedish Cancer Society SS 22 2023 Pj01H, SSSwedish Research Council 2019-05115, JLWallenberg Center for Protein Research - WCPR
6 · The paper itself

Abstract

Antibody prodrugs provide a strategy to reduce systemic toxicity by masking therapeutic antibodies until activation in specific physiological environments. Nivolumab, an anti-PD-1 checkpoint inhibitor used in cancer immunotherapy, can cause immune-related adverse events. As a first step toward a prodrug version of nivolumab, we screened an Escherichia coli affibody library using MACS and FACS, identifying affibodies that effectively mask its PD-1-binding regions. Deep sequencing revealed an unexpected enrichment of proline-rich variants, possibly mimicking a PD-1 loop. AlphaFold modeling suggested that these affibodies form interactions with nivolumab despite low alpha-helical content. Biosensor assays confirmed effective masking in a nivolumab prodrug format, with PD-1 binding restored upon proteolytic cleavage. These findings support further exploration of PD-1-mimicking affibodies as masking domains, advancing the development of more selective nivolumab prodrugs with improved safety profiles.

Indexed as

NivolumabProdrugsProtein EngineeringRecombinant Fusion ProteinsEscherichia coliHumansModels, MolecularProgrammed Cell Death 1 ReceptorProtein DomainsNivolumabProdrugsProgrammed Cell Death 1 ReceptorRecombinant Fusion Proteinsaffibody moleculebacterial displayconditional activationdirected evolutionnivolumabPD-1prodrug

Identifiers

PMID41989091
PMCPMC13122598

What OpenQuestion holds

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LicenceCC BY
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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.