Abstract
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°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 (DLarge). 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.
