ArticleNature biomedical engineering2025
Rapid clearance of achiral small-molecule drugs using de novo-designed proteins and their cyclic and mirror-image variants.
Article in Nature biomedical engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Redesign of the Ferritin Ferroxidase Center for Universal Molecular Binding or Specific Recognition.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Artificial intelligence in biologic drug discovery: A review of methodological evolution and therapeutic applications.Acta pharmaceutica Sinica. B · 2026Review
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Protein Structure Determination by Racemic and Quasi-Racemic X-Ray Crystallography.Chembiochem : a European journal of chemical biology · 2026Review
- Phytochemicals and REDOX Modulation: Molecular Mechanisms, Clinical Relevance, and Therapeutic Perspectives.Antioxidants (Basel, Switzerland) · 2026Review
- Deciphering DEL pocket patterns through contrastive learning.Nature communications · 2026Article
- De novo protein design: a transformative frontier in clinical protein applications.Journal of translational medicine · 2026Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Small-molecule-binding proteins can neutralize toxins and cytotoxic drugs, but their development is hindered by unpredictable in vivo behaviour and the poor immunogenicity of small molecules, which limits antibody-based approaches. Here we present a strategy to engineer de novo-designed proteins for the effective clearance of Food and Drug Administration-approved drugs in healthy mice. As a proof of concept, we designed proteins that bind to the anticoagulant apixaban. Since apixaban lacks chirality, we used mirror-image synthesis and cyclization to enhance the designed protein's in vivo stability. Both protein variants demonstrated effective activity, facilitating the rapid clearance of apixaban within 30 min. To assess the broader applicability of this approach, we extended our analysis to a de novo-designed protein targeting the anticancer drug rucaparib, further confirming its potential for small-molecule clearance. Our study shows that de novo-designed small-molecule-binding proteins can be used as antidotes in vivo, and that computational tools can be integrated with medicinal chemistry strategies for precise pharmacological interventions.
Indexed as
Identifiers
40442481What Socratic holds
Registered trials
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 Socratic graph.