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The incorporation of proteins into mesoporous silica, especially the SBA-15 (Santa Barbara Amorphous-15), stands out in biotechnology and in controlled drug delivery systems, due to its highly ordered mesoporous structure (with pore diameters between 5 to 30 nm), high surface area and outstanding thermal and chemical stability. Here, we have investigated the incorporation of antigenic proteins into distinct silicas, a process that can result in the adsorption or encapsulation of the biomolecule within the pores of the inorganic matrix. The silica-protein interaction can either preserve or alter the protein’s secondary structure, affecting its biological activity, while also protecting it against external agents such as pH variations and enzymatic degradation. The surface characteristics of the silica can influence protein conformation upon pore incorporation, potentially leading to partial loss of functional activity.
Notwithstanding these factors, SBA-15 demonstrates strong potential for use in biomedical applications, including the development of oral vaccines, since the encapsulation of proteins within mesoporous silica confers enhanced stability, preserves bioactivity, and facilitates controlled release. Furthermore, this system exhibits high loading capacity, excellent biocompatibility, and provides protection against denaturing agents.
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