Biological macromolecular machines perform impressive mechanical movements. F‐adenosine triphosphate (ATP) synthase uses a proton gradient to generate ATP through mechanical rotations. Here, a programmed hexagonal DNA nanomachine, in which a three‐armed DNA nanostructure (TAN) can perform stepwise rotations in the confined nanospace powered by DNA fuels, is demonstrated. The movement of TAN can precisely go through a 60° rotation, which is confirmed by atomic force microscopy, and each stepwise directional rotating is monitored by fluorescent measurements. Moreover, the rotary nanomachine is used to spatially organize cascade enzymes: glucose oxidase (GOx) and horseradish peroxidase (HRP) in four different arrangements. The multistep regulations of the biocatalytic activities are achieved by employing TAN rotations. This work presents a new prototype of rotary nanodevice with both angular and directional control, and provides a nanoscale mechanical engineering platform for the reactive molecular components, demonstrating that DNA‐based framework may have significant roles in futuristic nanofactory construction.

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A new type of thermoresponsive nanospheres was successfully developed by using a series of short intrinsically disordered polypeptide conjugated oligonucleotides as assembling building blocks.

Targeted protein degradation via proteasomal and lysosomal pathways is a promising therapeutic approach, and proteins in cytoplasm or on the cell membrane can be easily contacted and have become the major targets. However, degradation of disease‐related proteins that exist in membrane‐bound organelles (MBO) such as the endoplasmic reticulum (ER) remains unsolved due to the membrane limits. Here we describe a DNA nanodevice that shows ER targeting capacity and undergoes new intracellular degradation via the autophagy‐dependent pathway. Then the DNA nanostructure functionalized with specific ligands is used to selectively catch ER‐localized proteins and then transport them to the lysosome for degradation. Through this technique, the degradation of both exogenous ER‐resident protein (ER‐eGFP) and endogenous overexpressed molecular chaperone (glucose‐regulated protein 78) in cancer cells has been successfully executed with high efficiency.

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