AI-driven protein design and cell biophysics for therapeutics

The successful candidate will combine computational protein design with cell biology approaches to generate and characterize novel proteins with tailored functions. The project will involve the use of state-of-the-art design tools, including diffusion-based models and protein structure prediction approaches, to create candidate proteins. In parallel, the candidate will contribute to the development and implementation of cell biology assays to screen these candidates and characterize their functional properties in living cells. In particular, the project will focus on applications aimed at manipulating biomolecular condensates and pathological aggregates involved in neurodegenerative diseases.

Research environment: Our laboratory offers a highly collaborative and multidisciplinary environment with expertise in synthetic biology, biophysics, protein engineering, and cell biology. The candidate will benefit from access to state-of-the-art facilities and from regular interactions with researchers combining experimental and computational approaches.

The laboratory is located in the heart of Paris, within an exceptionally rich academic environment. The École Normale Supérieure and the broader PSL University ecosystem provide close proximity to internationally recognized research institutes, including Institut Curie, Collège de France, Institut Pasteur, and other leading centers in life sciences and quantitative biology.

Candidate profile: The applicant should hold a PhD in Synthetic Biology, Structural Biology, or Biophysics, and should demonstrate a strong interest in interdisciplinary and collaborative works.

Expected start date: October-December 2026. Applications (curriculum vitae, statement of research interests, and contact information of 2 references) should be addressed to: zoher.gueroui@ens.psl.eu

References

• De novo design of protein binders for programmable control of biomolecular condensates. Vu et al, https://www.cell.com/biophysj/abstract/S0006-3495(25)01637-6
• Phase-separated TDP-43 induces aggregation and reveals proteinopathy and cellular toxicity. Combe P, Subecz C, Le Goff G, Plamont MA, Bohl D, Gueroui Z. The FEBS Journal (2026). https://febs.onlinelibrary.wiley.com/doi/abs/10.1111/febs.70429
• Controlling lipid droplet dynamics via tether condensates. Amari C, Simon D, Bellon T, Plamont MA, Thiam AR, and Gueroui Z. Nat. Chem. Biol. (2025). https://www.nature.com/articles/s41589-025-01915-2