Redesign Protein Interfaces.
Reveal Hidden Hydrophobicity.
Use the physics of protein hydration to identify high-risk residues and design precise mitigations for aggregation and viscosity.
Solutions
Aggregation, high viscosity, and developability surprises are campaign-killers. You do not need another black-box score - you need residue-level maps of where the risk lives, and what to change.
Aggregation and stability
Prevent non-specific self-association that derails stability studies and forces late-stage reformulation.
High viscosity at dose
Identify physical drivers that limit concentration and complicate fill-finish and delivery.
Development yield and manufacturing pain
De-risk problem proteins early to avoid expensive iteration loops in process development and CMC.
PhiPI
PhiPI (Physics-informed Protein Interfaces) leverages an understanding of the complex physics of protein-water interactions to uncover hidden hydrophobic problem spots and suggest precision mitigations.
Physics-Grounded
All-atom phi-ensemble simulations map surface hydration thermodynamics to find the signal behind "hidden" hydrophobicity.
Neural-Speed
A proprietary GNN trained on physics truth produces high-fidelity maps in seconds, enabling fast iteration across variants.
Actionable Outputs
Patch overlays, ranked tables, and small mutation shortlists designed to plug into your existing assays.