RESUMO
Mesoporous silica spheres (SBA-15) have been obtained via a two-step synthesis process by using a triblock copolymer as a template in combination with a co-surfactant and co-solvent. Multi-amine-grafted mesoporous silicas were prepared by attaching 3-aminopropyl triethoxysilane, N-2(-aminoethyl)-3-aminopropyltrimethoxysilane and (3-trimethoxysilylpropyl)diethylenetriamine via a post-synthetic method. The proteins used in adsorption experiments include Bovine Serum Albumin (BSA), Lysozyme (LYS) and Myoglobin (MYO). The protein adsorption properties such as equilibrium and kinetics were investigated. The results show that the original SBA-15 samples have the highest adsorption capacity for all proteins due to their largest pore size and internal surface area.
Assuntos
Aminas/química , Cristalização/métodos , Nanosferas/química , Nanosferas/ultraestrutura , Nanotecnologia/métodos , Proteínas/química , Dióxido de Silício/química , Adsorção , Substâncias Macromoleculares/química , Teste de Materiais , Conformação Molecular , Tamanho da Partícula , Ligação Proteica , Propriedades de SuperfícieRESUMO
Based on morphology of SBA-15 particles, each has its own synthetic procedure and characteristics, resulting in different adsorption capacity as well as application in drug delivery system. This study focused on the synthesis mesoporous material SBA-15 with spherical morphology. The synthesized mesoporous silica SBA-15 were characterized by X-ray diffraction (XRD), transmission electron microscopy (TEM), scanning electron microscopy (SEM), fourier transform infrared (FT-IR), and BET analysis. The release study of original and modified samples were carried out to assess application for controlled drug delivery system. The adsorbed proteins can be readily desorbed on amine-modified samples. Especially, the diamine-modified sample has the highest release amount for two proteins, Lysozyme (LYS) and Myoglobin (MYO).