Related Experiment Video
Updated: Aug 13, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Reliability of AI Methods in Drug Discovery: Evaluation of Boltz-2 for Structure and Binding Affinity Prediction
Shunzhou Wan1, Xibei Zhang1, Xiao Xue1
1Centre for Computational Science, University College London, London, WC1H 0AJ, United Kingdom.
Abstract:
Despite continuing hype about the role of AI in drug discovery, no "AI-discovered drugs" have so far received regulatory approval. Here we assess one of the latest AI-based tools in this domain. Boltz-2, a recently developed biomolecular foundation model, aims to bridge the gap between AI efficiency and physics-based precision through a joint "cofolding" approach. In this study, we provide an extensive evaluation of Boltz-2 using two large-scale data sets: 16780 compounds for 3CLPro and 21702 compounds for TNKS2. We compare Boltz-2 predicted structures with traditional docking and binding affinities with binding free energies derived from the physics-based ESMACS protocol. Structural analysis reveals significant global RMSD variations, indicating that Boltz-2 predicts multiple protein conformations and ligand binding positions rather than a single converged pose. Energetic evaluations exhibit only weak to moderate correlations across the global data sets. Furthermore, a focused analysis of the top 100 compounds yields no significant correlation between the Boltz-2 predictions and the binding free energies from fine-grained ESMACS, alongside frequently observed saturation-state errors in Boltz-2 predicted ligand structures. Our results show that Boltz-2 lacks the energetic resolution required for lead identification. These findings highlight the necessity of employing physics-based methods for the reliability and refinement of AI-derived models.
Related Concept Videos
The Equilibrium Binding Constant and Binding Strength
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-Drug Binding: Determination Methods
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Ligand Binding and Linkage