Back

On improving experimental binding affinity predictions with synthetic data

Ryczko, K.; Zin, P. P.; Crivelli-Decker, J.; Le, L.; Jha, P. K.; Shields, B. J.; Lemos, P.; Bandi, S.; Van Damme, M.; Sood, A.; Huntington, L.; Pitman, M.; Ganahl, M.; Bortolato, A.

2026-03-04 molecular biology
10.64898/2026.03.02.708607 bioRxiv
Show abstract

The success of deep learning binding affinity prediction models depends critically on expanding experimental data with reliable synthetic data. We extend the Structurally Augmented IC50 Repository (SAIR) with {approx}80K absolute free energy perturbation (AFEP) calculations and present two distinct data splits, SAIR-FEP and SAIR-OOD (out-of-distribution), to simulate realistic drug discovery scenarios. We compare sequence-based proteochemometric (PCM) models and state-of-the-art, structure-based deep learning models and demonstrate that PCM models can be enhanced by physics-based descriptors. While structure-based deep learning methods capture finer geometric detail, their performance is highly sensitive to the input structure. By filtering for high-confidence, co-folded complexes, we show that the performance improves predictably, whereas training on all complexes blindly does not yield performance gains. Finally, using the SAIR-OOD split, we demonstrate that simultaneous training on synthetic and experimental data improves performance on publicly available, experimental benchmarks. These results provide a clear strategy for using synthetic data to advance experimental binding affinity predictions.

Matching journals

The top 6 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.