Bio-IT World reported on 22 September 2026 on results from the Federated OpenFold3 Initiative, run by Apheris through its AI Structural Biology network in collaboration with the AlQuraishi Lab at Columbia University, which develops OpenFold3. AbbVie, Astex Pharmaceuticals, Bristol Myers Squibb, Johnson & Johnson and Takeda each fine-tuned OpenFold3 Preview 2 locally inside their own environments on structures from active drug-discovery programs, with only model parameters periodically aggregated centrally; no structures were pooled. The combined training data spanned more than 20,000 experimentally determined protein-ligand structures, which the organizers state roughly triples the drug-relevant co-folding data available for training. The resulting model, AISB-1-Fed, is reported to outperform the foundation model it started from, every public model tested, and every model fine-tuned on a single partner's data alone, evaluated on 1,056 held-out private structures using the fraction of predictions meeting PL-lDDT of at least 0.8 and ligand RMSD within 2 Å. Nature covered the initiative on 14 September (Ewen Callaway, DOI: 10.1038/d41586-026-02882-x). The organizers' framing of why private data matters is itself notable: since the AlphaFold3 training cutoff the Protein Data Bank has grown by roughly 70,000 structures, but almost all are cofactors, metabolites, ions and crystallographic additives, with only around 10,600 public structures containing an approved or investigational drug and roughly 3,000 of those new since the cutoff. A follow-on effort, AISB Bind, extends the approach from structure to binding prediction with AbbVie, AstraZeneca, Bristol Myers Squibb and Johnson & Johnson. Contrary view: the results paper is not peer reviewed and was published on the vendor's own website, and Apheris is a commercial federated-computing provider with a direct interest in the finding that federation works. The benchmark consists of held-out private structures from the same five partners, so it measures fit to those companies' own medicinal-chemistry series rather than generalization to genuinely novel chemical space — the local-model problem that the Bender and colleagues Perspective covered in the prior cycle identifies as endemic. Dense analog series around targets a company already works on are exactly the data most likely to flatter a held-out split. Because the underlying structures and the trained weights remain private to participants, no external group can verify the result. And this remains structure prediction: the tracker has repeatedly noted that co-folding accuracy is an imperfect proxy for binding affinity, developability or in vivo behavior, and no evidence has been presented that the improvement changed a discovery decision.
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