Herre Jelger Risselada

The paper reconstructs lipidomic profiles from limited sequence data to reveal targeting patterns of therapeutic peptides and selectivity mechanisms of membrane-associated proteins.

The paper identifies a narrow thermodynamic design window for amphipathic peptides to selectively permeabilize viral membranes while sparing host cells, using a physics-driven generative workflow.

This paper identifies amphiphilic motifs that encode both fluid lyotropic phases and amyloid formation, linking functional condensation with pathological aggregation.

The paper shows Ups1 preferentially binds to positively curved membranes, facilitating phosphatidic acid transfer between mitochondrial membranes.