Among all cancers, lung cancer is one of the most common and serious types of cancer. It is challenging for site-specific delivery of anticancer therapeutics to tumor cells. Herein, we developed a novel“smart” dual-targeting liposomal platform to respond to the highly expressed hyaluronidase (HAase) in the tumor microenvironment and improve tumor targeting and antitumor efficacy.

As a highly pathogenic avian influenza virus, influenza A (H5N1) has been reported to infect humans, posing a major threat to both poultry industry and public health. It is an urgent need to develop a kind of effective vaccine to prevent death and reduce the incidence rate of H5N1 avian influenza. Compared with traditional inactivated or attenuated vaccines, deoxyribonucleic (DNA) vaccines have the advantages of continuously expressing plasmid-encoded antigens and inducing humoral and cellular immunity. However, the immune effect of DNA vaccines is limited to its poor immunogenicity. Using of nanoadjuvants with DNA vaccines holds a great promise to increase the transfection efficiency and immunogenicity of DNA vaccines. In this study, we developed a nano co-delivery system with a manganese-based liposome as adjuvant for delivery of a DNA vaccine. This system has been found to protect DNA vaccine, enhance phagocytosis as well as promote activation of antigen-presenting cells (APCs) and immune cells in draining lymph nodes. In addition, the effect of this nanovaccine has been evaluated in mouse models, where it induces highly potent hemagglutination inhibitory antibody (HI) and IgG antibodies, while activating both humoral and cellular immunity in the host. Overall, this strategy opens up a new prospect for manganese nanoadjuvants in increasing the immunogenicity of DNA vaccines.

Okara protein (OP) is a potential plant-based protein that is beneficial to human health. In this work, an alternating ultrasonic/alkali treatment method with non-continued cavitation and thermal energy output was used to extract protein (AUA-OP) from okara to enhance the functional properties of OP and improve the stability of OP-based emulsions. The purity of AUA-OP was greater than 80%. Compared with traditional (physical-assisted) alkali treatment, FTIR and SDS-PAGE revealed that AUA-OP retained the chemical structure of the protein, but the number of ultrasound-induced exposure sites increased, with increased fluorescence intensity, surface hydrophobicity, and absolute ζ-potential. After alternating ultrasonic/alkali treatment, the protein particles were looser and smaller. In addition, the water/oil holding capacity, EAI, and ESI of AUA-OP further increased. The viscosity of the AUA-OP-stabilized emulsion was also greater. Finally, a 28-day emulsion storage assay revealed that the AUA-OP-stabilized emulsion was stable with a relatively low droplet size and creaming index, indicating great potential for the development of stable protein-based emulsions.