One of the authors, VOK would like to thank University of Liège and VITO NV for financial support for his PhD. He is also grateful to Dr. V. Meynen (Univ. Antwerp), Dr. A. Buekenhoudt (VITO), H. Omari for valuable discussions and technical staff of the Materials Technology department of VITO for their help in characterization. Supporting Information is available from the Wiley Online Library or from the author.
Systematic Processing of β-Tricalcium Phosphate for Efficient Protein Loading and In Vitro Analysis of Antigen Uptake†
Article first published online: 22 NOV 2012
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Advanced Engineering Materials
Volume 15, Issue 4, pages 295–301, April 2013
How to Cite
Ozhukil Kollath, V., De Geest, B. G., Mullens, S., De Koker, S., Luyten, J., Persoons, R., Traina, K., Remon, J. P. and Cloots, R. (2013), Systematic Processing of β-Tricalcium Phosphate for Efficient Protein Loading and In Vitro Analysis of Antigen Uptake. Adv. Eng. Mater., 15: 295–301. doi: 10.1002/adem.201200177
- Issue published online: 8 APR 2013
- Article first published online: 22 NOV 2012
- Manuscript Accepted: 2 OCT 2012
- Manuscript Received: 14 MAY 2012
- University of Liège and VITO NV
Microparticulate calcium phosphate (CaP) powders are promising drug carriers because of their biocompatibility and degradability under physiological conditions. The adsorption capability of CaP microparticles makes them interesting candidates, within the inorganic carrier materials, for delivering protein antigens to professional antigen presenting cells (APC) for vaccination purpose. However, in order to bind and deliver a sufficient amount of protein, the challenge is to effectively increase the binding capacity of this material. In this study, β-tricalcium phosphate (β-TCP) powder is engineered to obtain microparticles with increased protein loading, using bovine serum albumin as a model antigen. The decrease in particle size and increase in specific surface area of carrier is shown to strongly affect protein adsorption. Finally, we demonstrate that the processed β-TCP is capable of delivering its protein payload in vitro to dendritic cells, which are professional APCs and the target cell population for microparticulate vaccines.