Evidence map›Paper›PMID 40170886›Full record

ArticleBioinformatics advances2025

AntiFold: improved structure-based antibody design using inverse folding.

Magnus Haraldson Høie, Alissa M Hummer, Tobias H Olsen, Broncio Aguilar-Sanjuan, Morten Nielsen, Charlotte M Deane

Abstract read
In one paragraph

Article in Bioinformatics advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  5. Article
  6. Article
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  8. Article
  9. Article
  10. AI-Driven De Novo Binder Design: From Structure Prediction to Closed-Loop Optimization.Computational and structural biotechnology journal · 2026
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. AntiBMPNN: Structure-Guided Graph Neural Networks for Precision Antibody Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  19. Review
  20. 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.

Magnus Haraldson HøieSection for Bioinformatics, Department of Health Technology, Technical University of Denmark, Lyngby DK-2800, Denmark.ORCID https://orcid.org/0000-0003-2567-758X
Alissa M HummerDepartment of Statistics, University of Oxford, Oxford OX1 3LB, United Kingdom.ORCID https://orcid.org/0000-0002-3023-2588
Tobias H OlsenDepartment of Statistics, University of Oxford, Oxford OX1 3LB, United Kingdom.ORCID https://orcid.org/0000-0002-6348-4650
Broncio Aguilar-SanjuanDepartment of Statistics, University of Oxford, Oxford OX1 3LB, United Kingdom.ORCID https://orcid.org/0000-0001-8068-6417
Morten NielsenSection for Bioinformatics, Department of Health Technology, Technical University of Denmark, Lyngby DK-2800, Denmark.ORCID https://orcid.org/0000-0001-7885-4311
Charlotte M DeaneDepartment of Statistics, University of Oxford, Oxford OX1 3LB, United Kingdom.ORCID https://orcid.org/0000-0003-1388-2252

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Summary: The design and optimization of antibodies requires an intricate balance across multiple properties. Protein inverse folding models, capable of generating diverse sequences folding into the same structure, are promising tools for maintaining structural integrity during antibody design. Here, we present AntiFold, an antibody-specific inverse folding model, fine-tuned from ESM-IF1 on solved and predicted antibody structures. AntiFold outperforms existing inverse folding tools on sequence recovery across complementarity-determining regions, with designed sequences showing high structural similarity to their solved counterpart. It additionally achieves stronger correlations when predicting antibody-antigen binding affinity in a zero-shot manner. AntiFold assigns low probabilities to mutations that disrupt antigen binding, synergizing with protein language model residue probabilities, and demonstrates promise for guiding antibody optimization while retaining structure-related properties. Availability and implementation: AntiFold is freely available under the BSD 3-Clause as a web server (https://opig.stats.ox.ac.uk/webapps/antifold/) and pip-installable package (https://github.com/oxpig/AntiFold).

Identifiers

PMID40170886
PMCPMC11961221

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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.