Abstract
Biological membranes achieve selectivity and permeability through protein transporters and channels. The design of artificial compartments with permeable membranes is essential to facilitate substrate and product transfer in enzymatic reactions. In this study, an E. coli outer membrane protein OmpF fused to a modular adaptor was integrated onto a DNA origami skeleton to control the number and polarity of the OmpF trimer. DNA origami skeleton-guided nanoliposomes reconstituted with functional OmpF exhibit pH-responsiveness and size-selective permeability. This approach highlights the potential to construct artificial compartments that incorporate membrane proteins of defined number and polarity, allowing tunable substrate fluxes.