top of page

Credits: Anthony Schuller

The Nuclear Pore Complex (NPC) is the largest protein complex in the cell. About 1000 proteins make up this wonderful structure, which perforates the double-membrane structure of the nuclear envelope and mediates selective exchange of proteins and RNA between nucleoplasm and cytoplasm.

Credits: Nicola De Franceschi

Our collaborators from the Dietz Lab (TUM) have designed and produced a synthetic version of the NPC made of DNA origami. 

As a compelling demonstration of the level of  programmability that can be achieved using DNA origami, this pore matches the size and geometry of a real NPC. 

Cholesterol groups (indicated in red) allowed us to reconstitute this synthetic NPC in giant liposomes.


To the interior of the ring, attachment site for spaghetti-like proteins, called Nups, will allow to reconstitute selective transport across the pore.

Work done in the Dekker Lab in collaboration with the Dietz lab.

And here's the pore in action.

A large, hydrophilic protein such as GFP can enter the lumen of the liposome by crossing the membrane via the synthetic NPC pore.

Fragasso & De Franceschi & Stommer et al.

 ACSnano 2021

bottom of page