Protein–Peptide Docking with ESMFold Language Model
Designing peptide therapeutics requires precise peptide docking, which remains a challenge. We assessed the ESMFold language model, originally designed for protein structure prediction, for its effectiveness in protein-peptide docking. Various docking strategies, including polyglycine linkers and sampling-enhancing modifications, were explored. The number of acceptable-quality models among top-ranking results is comparable to traditional methods and generally lower than AlphaFold-Multimer or Alphafold 3, though ESMFold surpasses it in some cases. The combination of result quality and computational efficiency underscores ESMFold's potential value as a component in a consensus approach for high-throughput peptide design.
Authors
- Sebastian Kmiecik (ORCID: https://orcid.org/0000-0001-7623-0935)
- Mateusz Zalewski (ORCID: https://orcid.org/0000-0002-3436-8829)
- Björn Wallner (ORCID: https://orcid.org/0000-0002-3772-8279)
Institutions
- Linköping University (SE)
- University of Warsaw (PL)
Publication Details
- Journal
- Journal of Chemical Theory and Computation
- Published
- 2025-03-07
- DOI
- https://doi.org/10.1021/acs.jctc.4c01585
- Citations
- 12
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 9.67
Funders
- Narodowe Centrum Nauki