Protein loaded mesoporous silica spheres as a controlled delivery platform

Ho, Jenny, Danquah, Michael K., Wang, Huanting, & Forde, Gareth M. (2008) Protein loaded mesoporous silica spheres as a controlled delivery platform. Journal of Chemcial Technology and Biotechnology, 83(3), pp. 351-358.

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The adsorption of bovine serum albumin (BSA) onto mesoporous silica spheres (MPS) synthesized from silica colloids was studied employing real time in situ measurements. The stabilities of the BSA at different pH values, their isoelectric points and zeta potentials were determined in order to probe the interactions between the protein and the mesoporous silica.


The pore size of MPS was designed for protein, and this, coupled with an in depth understanding of the physico-chemical characteristics of the protein and MPS has yielded a better binding capacity and delivery profile. The adsorption isotherm at pH 4.2 fitted the Langmuir model and displayed the highest adsorption capacity (71.43 mg mL-1 MPS). Furthermore, the delivery rates of BSA from the MPS under physiological conditions were shown to be dependent on the ionic strength of the buffer and protein loading concentration.


Economics and scale-up considerations of mesoporous material synthesized via destabilization of colloids by electrolyte indicate the scaleability and commercial viability of this technology as a delivery platform for biopharmaceutical applications.

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25 citations in Scopus
24 citations in Web of Science®
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ID Code: 81546
Item Type: Journal Article
Refereed: Yes
Keywords: Colloidal silica, In vitro delivery studies, Mesoporous silica sphere, Protein adsorption, Protein delivery platform, Adsorption isotherms, Colloids, Drug products, Electrolytes, Mesoporous materials, pH, Proteins, Silica, Zeta potential, Biopharmaceutical application, Delivery platform, Isoelectric points, Controlled drug delivery, bovine serum albumin, drug, silicon dioxide, adsorption kinetics, article, drug delivery system, in vitro study, isoelectric point, physical chemistry, porosity, protein binding, protein expression, protein interaction, protein stability, protein synthesis, surface property, Bovinae
DOI: 10.1002/jctb.1818
ISSN: 0268-2575
Divisions: Current > Schools > School of Chemistry, Physics & Mechanical Engineering
Current > QUT Faculties and Divisions > Science & Engineering Faculty
Deposited On: 05 Feb 2015 23:32
Last Modified: 11 Feb 2015 03:38

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