Research and engineering programme · NVIDIA · 2023–2024

Protein inverse folding for peptide design

An eight-person programme combining ProteinMPNN fine-tuning, diversity-regularised direct preference optimisation and sequence–structure evaluation.

Problem

Inverse-folding systems can generate sequences compatible with a target backbone while concentrating on a narrow part of sequence space. For peptide design, increasing diversity is useful only if the generated sequences retain the required structural similarity.

Method

The team fine-tuned ProteinMPNN and applied direct preference optimisation with an explicit diversity regulariser. Evaluation paired sequence-diversity measures with structure-based checks so that improvement in one objective was not reported without the other.

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Conceptual pipeline: target backbone, candidate sequences and diversity-aware selection with structural checks.

My role

As Global Life Sciences Research Alliances Lead, I managed the eight-person science and engineering team. I coordinated the work on model fine-tuning, preference optimisation and evaluation through to publication.

Collaborators

The paper was authored by Ryan Park, Darren J. Hsu, C. Brian Roland, Maria Korshunova, Chen Tessler, Shie Mannor, Olivia Viessmann and Bruno Trentini.

Result

The reported method improved sequence diversity by 20% while maintaining structural similarity. The work was selected as a spotlight at the ICML 2025 2nd Workshop on Generative AI and Biology.

8researchers and engineers
20%higher sequence diversity
SpotlightICML 2025 GenBio workshop