An average cell contains thousands of proteins that participate in normal cellular functions, and most diseases are somehow related to the malfunctioning of one or more of these proteins. Protein therapy, which delivers proteins into the cell to replace the dysfunctional protein, is considered the most direct and safe approach for treating disease. However, the effectiveness of this method has been limited by its low delivery efficiency and poor stability against proteases in the cell, which digest the protein. Here, we show a novel delivery platform based on nanocapsules consisting of a protein core and a thin permeable polymeric shell that can be engineered to either degrade or remain stable at different pHs. Non-degradable capsules show long-term stability, whereas the degradable ones break down their shells, enabling the core protein to be active once inside the cells. Multiple proteins can be delivered to cells with high efficiency while maintaining low toxicity, suggesting potential applications in imaging, therapy and cosmetics fields.

Single protein encapsulated into nanogels with uniformed size and controllable shell thickness were prepared by surface acryloylation of a protein molecule followed by aqueous in situ polymerization. Compared to its free counterpart, the encapsulated protein exhibits similar biocatalytic behavior and significantly improved stability at high temperature and in the presence of organic solvent.

No abstract

Organisms have sophisticated subcellular compartments containing enzymes that function in tandem. These confined compartments ensure effective chemical transformation and transport of molecules, and the elimination of toxic metabolic wastes1,2. Creating functional enzyme complexes that are confined in a similar way remains challenging. Here we show that two or more enzymes with complementary functions can be assembled and encapsulated within a thin polymer shell to form enzyme nanocomplexes. These nanocomplexes exhibit improved catalytic efficiency and enhanced stability when compared with free enzymes. Furthermore, the co-localized enzymes display complementary functions, whereby toxic intermediates generated by one enzyme can be promptly eliminated by another enzyme. We show that nanocomplexes containing alcohol oxidase and catalase could reduce blood alcohol levels in intoxicated mice, offering an alternative antidote and prophylactic for alcohol intoxication.

Searching the high‐efficient, stable, and earth‐abundant electrocatalysts to replace the precious noble metals holds the promise for practical utilizations of hydrogen and oxygen evolution reactions (HER and OER). Here, a series of highly active and robust Co‐doped nickel phosphides (Ni2−xCoxP) catalysts and their hybrids with reduced graphene oxide (rGO) are developed as bifunctional catalysts for both HER and OER. The Co‐doping in Ni2P and their hybridization with rGO effectively regulate the catalytic activity of the surface active sites, accelerate the charge transfer, and boost their superior catalytic activity. Density functional theory calculations show that the Co‐doped catalysts deliver the moderate trapping of atomic hydrogen and facile desorption of the generated H2 due to the H‐poisoned surface active sites of Ni2−xCoxP under the real catalytic process. Electrochemical measurements reveal the high HER efficiency and durability of the NiCoP/rGO hybrids in electrolytes with pH 0–14. Coupled with the remarkable and robust OER activity of the NiCoP/rGO hybrids, the practical utilization of the NiCoP/rGO‖NiCoP/rGO for overall water splitting yields a catalytic current density of 10 mA cm−2 at 1.59 V over 75 h without an obvious degradation and Faradic efficiency of ≈100% in a two‐electrode configuration and 1.0 m KOH.