Achieving autonomous motion is a central objective in designing artificial cells that mimic biological cells in form and function. Cellular motion often involves complex multiprotein machineries, which are challenging to reconstitute in vitro. Here we achieve persistent motion of cell-sized liposomes. These small artificial vesicles are driven by a direct mechanochemical feedback loop between the MinD and MinE protein systems of Escherichia coli and the liposome membrane. Membrane-binding Min proteins self-organize asymmetrically around the liposomes, which results in shape deformation and generates a mechanical force gradient leading to motion. The protein distribution responds to the deformed liposome shape through the inherent geometry sensitivity of the reaction–diffusion dynamics of the Min proteins. We show that such a mechanochemical feedback loop between liposome and Min proteins is sufficient to drive continuous motion. Our combined experimental and theoretical study provides a starting point for the future design of motility features in artificial cells.

The MinDE proteins from E. coli have received great attention as a paradigmatic biological pattern-forming system. Recently, it has surfaced that these proteins do not only generate oscillating concentration gradients driven by ATP hydrolysis, but that they can reversibly deform giant vesicles. In order to explore the potential of Min proteins to actually perform mechanical work, we introduce a new model membrane system, flat vesicle stacks on top of a supported lipid bilayer. MinDE oscillations can repeatedly deform these flat vesicles into tubules and promote progressive membrane spreading through membrane adhesion. Dependent on membrane and buffer compositions, Min oscillations further induce robust bud formation. Altogether, we demonstrate that under specific conditions, MinDE self-organization can result in work performed on biomimetic systems and achieve a straightforward mechanochemical coupling between the MinDE biochemical reaction cycle and membrane transformation.

Inspired by the self-assembly phenomena in nature, the instructed self-assembly of exogenous small molecules in a biological environment has become a prevalent process to control cell fate. Despite mounting examples of versatile bioactivities, the underlying mechanism remains less understood, which is in large hindered by the difficulties in the identification of those dynamic assemblies in situ. Here, with direct stochastic optical reconstruction microscopy, we are able to elucidate the dynamic morphology transformation of the enzyme-instructed supramolecular assemblies in situ inside cancer cells with a resolution below 50 nm. It indicates that the assembling molecules endure drastically different pathways between cell lines with different phosphatase activities and distribution. In HeLa cells, the direct formation of intracellular supramolecular nanofibers showed slight cytotoxicity, which was due to the possible cellular secretory pathway to excrete those exogenous molecules assemblies. In contrast, in Saos-2 cells with active phosphatase on the cell surface, assemblies with granular morphology first formed on the cell membranes, followed by a transformation into nanofibers and accumulation in cells, which induced Saos-2 cell death eventually. Overall, we provided a convenient method to reveal the in situ dynamic nanomorphology transformation of the supramolecular assemblies in a biological environment, in order to decipher their diverse biological activities.

Self-reproduction is one of the most important characteristics of lipid vesicles for origin of life research. Most vesicle self-reproduction systems are based on fatty acid vesicles and spontaneous phospholipid vesicle production is difficult owing to the relatively high stability of these vesicles. Now, spontaneous phospholipid vesicle generation and extension in a dipeptide/phospholipid system is demonstrated. Dissolution of the dipeptide crystal provides both the driving force and phospholipid constituents for vesicle generation and extension. This study provides a new system to enhance the understanding of vesicle self-reproduction mechanisms.

DNA nanostructures are promising biomaterials capable of arranging multiple functional components with nanometer precision. Here, a double-bundle DNA tetrahedron is rationally designed to integrate with antisense oligonucleotides silencing proto-oncogene c-raf and nuclear targeting peptides. The functionalized DNA tetrahedron can be internalized by A549 cells and assists the delivery of antisense oligonucleotides toward the nucleus to increase the chance to downregulate target mRNA in nucleus and cytoplasm. Antisense strands released from the tetrahedron in response to the intracellular reducing environment can inhibit cell proliferation at a low concentration without transfection reagent. Finally, efficient knockdown of c-raf gene is observed, which verified our design. This designer DNA-based nanocarrier system will open a new avenue for efficient delivery of nucleic acid drugs.

Controlled growth of one-dimensional nanostructures is playing a key role in creating types of materials for functional devices. Here, we report procedures for controlled assembly of the dipeptide diphenylalanine (FF) into aligned and ultralong single crystals in a capillary. With the evaporation of solvent, nucleation of the crystal occurred in the confined region, and the crystal grew continuously with a supply of molecules from the concentration gradient system inside the capillary. Based on the "Knudsen regime", an ultralong aligned individual FF single crystal possessing an active optical waveguide property at macroscopic length scale could be obtained. Moreover, capillary is also an effective microdevice to investigate the disassembly process of the FF single crystals. This strategy has potentials to broaden the range of applications of aligned organic nanomaterials.

Coupling between cytoskeleton and membranes is critical to cell movement as well as organelle formation. Here, we demonstrate that self-assembled single crystals of a dipeptide, diphenylalanine (FF), can interact with liposomes to form cytoskeleton-like structures. Under a physiological condition, disassembly of FF crystals deforms and translocates supported lipid membrane. The system exhibits similar dynamic characteristics to the endoplasmic reticulum (ER) network in cells. This bottom-up system thus indicates that external matter can participate in the deformation of liposomes, and disassembly of the nanostructures enables a system with distinct dynamic behaviors.

We obtained the fluorescence localization images of tube DNA origami nanostructures in NIH 3T3 cells for the first time. The fluorescence localization images of tube DNA origami nanostructures and TIRF images of lysosomes were combined and they revealed the detailed interactions between the two structures. Quantitative analysis illustrated that the tube origami can be captured as well as degraded by lysosomes with time.

Biological organic-inorganic hybrid materials often achieve excellent properties and provide inspiration for the design of advanced materials. The organic phase plays a key role in determining the properties of biogenic materials, and the spatial arrangement of organic and inorganic phases provides direct evidence for interaction between the two phases. Super-resolution fluorescence microscopy was used to visualize the gelatin distribution in two different crystalline polymorphs of calcium carbonate (vaterite and calcite) and to investigate the process by which gelatin is excluded from the crystals. The results demonstrated that gelatin is distributed through vaterite microspheres in the form of nanoparticles, whereas it tends to accumulate on the edges of the calcite rhombohedra.