Surface polymer engineering was applied with a carrier of exosomes, namely, the amphiphilic cationic CHP (cCHP) nanogel, to improve the delivery of exosome content by forming complexes with the exosomes.

Chlorins with phenol units were dissolved in water via complexation with the solubilizing agents trimethyl-β-cyclodextrin and λ-carrageenan using a high-speed vibration milling technique. The photodynamic activities of the trimethyl-β-cyclodextrin (TMeβCD) and λ-carrageenan complexes were similar to that of Photofrin. However, the λ-carrageenan chlorin complexes were more stable in aqueous solutions than the TMeβCD–chlorin complexes. Thus, λ-carrageenan-complexed chlorin would be more suitable as a photosensitizer.

β‐(1,3‐1,6)‐D‐Glucan, λ‐carrageenan, tamarind gum, and pullulan can dissolve various porphyrin derivatives via the formation of complexes in water using a high‐speed vibration milling method. The aqueous solutions of the resulting complexes exhibit long‐term stability. Despite the adverse effects of the self‐quenching process, notable fluorescence and improved photodynamic activity of the polysaccharide‐complexed porphyrin derivatives were observed in the presence of liposomes, micelles, cyclodextrins, and HeLa cells. It was noted that the type of porphyrins was more important than the type of polysaccharides present in the complex. Porphyrin self‐aggregates were monodispersed in the lipid membranes of the liposomes and lysosomes. The polysaccharide‐complexed porphyrin derivatives showed increased photodynamic activity toward HeLa cells under photoirradiation between 610 and 740 nm.

Protein pharmaceuticals show great therapeutic promise, but effective intracellular delivery remains challenging. To address the need for efficient protein transduction systems, we used a magnetic nanogel chaperone (MC): a hybrid of a polysaccharide nanogel, a protein carrier with molecular chaperone-like properties, and iron oxide nanoparticles, enabling magnetically guided delivery. The MC complexed with model proteins, such as BSA and insulin, and was not cytotoxic. Cargo proteins were delivered to the target HeLa cell cytosol using a magnetic field to promote movement of the protein complex toward the cells. Delivery was confirmed by fluorescence microscopy and flow cytometry. Delivered β-galactosidase, inactive within the MC complex, became enzymatically active within cells to convert a prodrug. Thus, cargo proteins were released from MC complexes through exchange interactions with cytosolic proteins. The MC is a promising tool for realizing the therapeutic potential of proteins.