Dynamic control of nanofluidic channels in protein drug delivery vehicles

Proteocubosomic nanocarriers are three-dimensional (3D) self-assembly periodic nanofluidic structures that have a surface topology of open nanochannels, which is apparent also in natural and self-assembled viral capsids. Here, proteins are nanoconfined in a hydrated self-assembly mixture of amphiphilic monoolein (MO) and octylglucoside (OG) forming cubosomic nanostructures. The generated periodic 3D nanochannel network architectures are investigated by means of synchrotron X-ray diffraction. The structural behavior of the ternary MO/OG/transferrin and MO/OG immunoglobulin systems as well as the binary MO/OG mixture is studied in excess aqueous environment in the temperature range from 1 to 99 degrees C. The results indicate that 5% OG molar fraction in protein-containing monoolein systems favors the formation of a swollen bicontinuous cubic liquid crystalline structure with large water channels (D-Large). Thus, it is feasible to dynamically adjust the diameters of the nanofluidic aqueous channels in the proteocubosomic carrier via the incorporation of a suitable amphiphilic additive. The obtained results may inspire the development of novel stimuli-responsive protein drug delivery nanovehicles and biocompatible self-regulating nanofluidic devices.