Application Of Functionalized Mesoporous Silica Nanoparticles On Adsorption And Separation Of Proteins

Mesoporous silica nanoparticles (MSNs) show many excellent characteristics, such as good biocompatibility, chemical stability, high surface areas, large pore volumes, uniform and tunable pore sizes and so on. Furthermore, MSNs can be flexibly surface-modified with a variety of organic functionalities. The mesoporous organic-inorganic hybrid materials is typically carried out using the one-pot synthesis (co-condensation), post synthesis (grafting), and PMOs (Periodic Mesoporous Organicsilica) synthesis method. Functionalized MSNs enlarge the application of materials and improve the adsorption and release of biomolecules. On the basis of the previous researches, the following innovative works were carried out:(1)Sulfonic acid-functionalized SBA-15mesoporous molecular sieve (SBA-15-SO3H and SBA-15-po-SO3H) were synthesized by two kinds of post-synthesis methods. The functionalized SBA-15materials were characterized and used to study the adsorption behavior for polypeptides (insulin and glucagon) and proteins (bovine serum albumin and cytochrome c) in the static and dynamic processes. The two kinds of functionalized SBA-15mesoporous materials showed selectively adsorption of proteins in the dynamic adsorption mode.(2)The mesostructural order of Periodic Mesoporous Organosilicas (PMO) with an organobridged (-CH2-) was synthesized and functionalized with amino or carboxylic group by post-synthesis methods. These PMO materials were used for the adsorption of proteins with different isoelectric point (pI). The adsorption of proteins on PMO materials were affected by not only experimental conditions, the structure and the function groups of materials and shapes of proteins, but also the sample constitutes.(3)Protein-drug interaction is significant in pharmacology and it is important to understand the different binding functions of anticancer drug to transport protein. Interaction of lycorine or tamoxifen citrate with bovine serum albumin (BSA) was investigated by various spectroscopic analysis methods under simulative physiological conditions. The results showed that the two kinds of interaction were with completely different binding modes.