Bioadsorption of proteins on large mesocage-shaped mesoporous alumina monoliths.

With the remarkable progress in the field of gene technology, proteins have gained an important function in the field of disease diagnosis and treatment. Protein bioadsorption has drawn increasing attention partly because of the promising advances for diagnostic assays, sensors, separations, and gene technology. Mesocage alumina has a cage-type structure with high surface area and pore volume, exhibiting superior capabilities for protein adsorption. In this study, we report the size-selective adsorption/removal of virtual proteins having different shapes, sizes, functions, and properties, including insulin, HopPmaL domain, lysozyme, galectin-3, β-lactoglobulin, α-1-antitrypsin, α-amylase, and myosin in aqueous water using mesocage alumina. The mesoporous alumina monoliths have unique morphology and physical properties and enhanced protein adsorption characteristics in terms of sample loading capacity and quantity, thereby ensuring a higher concentration of proteins, interior pore diffusivity, and encapsulation in a short period. Thermodynamic analysis shows that protein adsorption on mesocage alumina monoliths is favorable and spontaneous. Theoretical models have been studied to investigate the major driving forces to achieve the most optimal performance of protein adsorption. The development of ultra- or micrometer-scale morphology composed of mesocage-shaped mesoporous monoliths or alumina network clusters can be effectively used to encapsulate the macromolecules into the interior cage cavities, which can greatly assist in other potentials for biomedical applications. Furthermore, the adsorption of a single protein from mixtures based on size- and shape-selective separation can open up new ways to produce micro-objects that suit a given protein encapsulation design.