Preparation and Release Properties of Sol-Gel Encapsulated Proteins
Affiliation(s)
Department of Chemistry, National Taiwan University, Taipei, Taiwan. Department of Food Science/Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan. Department of Biology, Georgia State University, Atlanta, USA.
Department of Chemistry, National Taiwan University, Taipei, Taiwan. Department of Food Science/Biological Science and Technology, China University of Science and Technology, Taipei, Taiwan. Department of Biology, Georgia State University, Atlanta, USA.
ABSTRACT
A glycoprotein, bovine serum albumin
(BSA) was used as a model compound for encapsulation in a sol-gel matrix. Dried
gels were ground into powders and meshed to achieve particle sizes less than
250 μm. The products were washed with phosphate buffer. Capillary
electrophoresis was used to evaluate the encapsulation efficiency and the
kinetic properties of protein release. Several parameters, including the pH and
composition of the background electrolyte, were investigated in an effort to
eliminate the matrix effect from the determination of release kinetics.
Complete separation of the silica matrix from BSA was using phosphate buffer, an
applied voltage of 15 kV, and detection at 278 nm. Kinetic studies indicated
that most of the BSA was released in the first 5 h. The rate of BSA release gradually
decreased, and some BSA after 25 h. These results indicated that dilute potassium phosphate buffer could accelerate
protein release, but this was not observed for the concentrations greater than
50 mM. We believe the developed method has potential utility in other systems for in vitro matrix
dissolution and drug release studies.
Cite this paper
Y. Chen, C. Liu, C. Yang, B. Huang and C. Liu, "Preparation and Release Properties of Sol-Gel Encapsulated Proteins," Journal of Analytical Sciences, Methods and Instrumentation, Vol. 3 No. 3, 2013, pp. 11-16. doi: 10.4236/jasmi.2013.33A002.
Y. Chen, C. Liu, C. Yang, B. Huang and C. Liu, "Preparation and Release Properties of Sol-Gel Encapsulated Proteins," Journal of Analytical Sciences, Methods and Instrumentation, Vol. 3 No. 3, 2013, pp. 11-16. doi: 10.4236/jasmi.2013.33A002.
References
[1] R. Haag and F. Kratz, “Polymer Therapeutics: Concepts and Applications,” Angewandte Chemie, Vol. 45, No. 8, 2006, pp. 1198-1215. http://dx.doi.org/10.1002/anie.200502113 [2] M. Molinos, V. Carvalho, D. M. Silva and F. M. Gama, “Development of a Hybrid Dextrin Hydrogel Encapsulating Dextrin Nanogel as Protein Delivery System,” Biomacromolecules, Vol. 13, No. 2, 2012, pp. 517-527. http://dx.doi.org/10.1021/bm2015834 [3] G. J. Hickman, A. Rai, D. J. Boocock, R. C. Rees and C. C. Perry, “Fabrication, Characterisation and Performance of Hydrophilic and Superhydrophilic Silica as Cell Culture Surfaces,” Journal of Materials Chemistry, Vol. 22, No. 24, 2012, pp. 12141-12148. http://dx.doi.org/10.1039/c2jm31161e [4] M. R. N. Monton, E. M. Forsberg and J. D. Brennan, “Tailoring Sol-Gel-Derived Silica Materials for Optical Biosensing,” Chemistry of Materials, Vol. 24, No. 5, 2012, pp. 796-811. http://dx.doi.org/10.1021/cm202798e [5] W. Jin and J. D. Brennan, “Properties and Applications of Proteins Encapsulated within Sol-Gel Derived Materials,” Analytica Chimica Acta, Vol. 461, No. 1, 2002, pp. 1-36. http://dx.doi.org/10.1016/S0003-2670(02)00229-5 [6] I. Gill, “Bio-Doped Nanocomposite Polymers: Sol-Gel Bioencapsulates,” Chemistry of Materials, Vol. 13, No. 10, 2001, pp. 3404-3421. http://dx.doi.org/10.1021/cm0102483 [7] C. P. Liu and S. D. Liu, “Formulation and Characterization of the Microencapsulated Entomopathogenic Fungus Metarhizium anisopliae MA126,” Journal of Microencapsulation, Vol. 26, No. 5, 2009, pp. 377-384. http://dx.doi.org/10.1080/02652040802365455 [8] M. Kato, K. Inuzuka, K. Sakai-Kato and T. Toyo’oka, “Monolithic Bioreactor Immobilizing Trypsin for High-Throughput Analysis,” Analytical Chemistry, Vol. 77, No. 6, 2005, pp. 1813-1818. http://dx.doi.org/10.1021/ac048388u [9] S. Murayama, F. Ishizuka, K. Takagi, H. Inoda, A. Sano, T. Santa and M. Kato, “Small Mesh Size Hydrogel for Functional Photocontrol of Encapsulated Enzymes and Small Probe Molecules,” Analytical Chemistry, Vol. 84, No. 3, 2012, pp. 1374-1379. http://dx.doi.org/10.1021/ac2023603 [10] D. J. Dickson and R. L. Ely, “Silica Sol-Gel Encapsulation of Cyanobacteria: Lessons for Academic and Applied Research,” Applied Microbiology and Biotechnology, Vol. 97, No. 5, 2013, pp. 1809-1819. http://dx.doi.org/10.1007/s00253-012-4686-8 [11] N. Bhattarai, H. R. Ramay, J. Gunn, F. A. Matsen and M. Zhang, “PEG-Grafted Chitosan as an Injectable Thermosensitive Hydrogel for Sustained Protein Release,” Journal of Controlled Release, Vol. 103, No. 3, 2005, pp. 609-624. http://dx.doi.org/10.1016/j.jconrel.2004.12.019 [12] L. E. Vera-Avila, E. García-Salgado, M. P. García de Llasera and A. Pena-Alvarez, “Binding Characteristics of Bovine Serum Albumin Encapsulated in Sol-Gel Glasses: An Alternative for Protein Interaction Studies,” Analytical Biochemistry, Vol. 373, No. 2, 2008, pp. 272-280. http://dx.doi.org/10.1016/j.ab.2007.08.036 [13] C. D. Tran, D. Ilieva and S. Challa, “Inhomogeneity in Distribution and Conformation of Bovine Serum Albumin in Sol-Gel: A Closer Look with a Near-Infrared Multispectral Imaging Technique,” Journal of Sol-Gel Science and Technology, Vol. 32, No. 1-3, 2004, pp. 207-217. http://dx.doi.org/10.1007/s10971-004-5790-8 [14] Y. Gao, A. Heinemann, R. Knott and J. Bartlett, “Encapsulation of Protein in Silica Matrices: Structural Evolution on the Molecular and Nanoscales,” Langmuir, Vol. 26, No. 2, 2010, pp. 1239-1246. http://dx.doi.org/10.1021/la9023986 [15] M. Kato, K. Sakai-Kato, N. Matsumoto and T. Toyo’oka, “A Protein-Encapsulation Technique by the Sol-Gel Method for the Preparation of Monolithic Columns for Capillary Electrochromatography,” Analytical Chemistry, Vol. 74, No. 8, 2002, pp. 1915-1921. http://dx.doi.org/10.1021/ac0112162 [16] M. Kato, N. Matsumoto, K. Sakai-Kato and T. Toyo’oka, “Investigation of Chromatographic Performances and Binding Characteristics of BSA-Encapsulated Capillary Column Prepared by the Sol-Gel Method,” Journal of Pharmaceutical and Biomedical Analysis, Vol. 30, No. 6, 2003, pp. 1845-1850. http://dx.doi.org/10.1016/S0731-7085(02)00527-7 [17] M. Kato, H. Saruwatari, K. Sakai-Kato and T. Toyo’oka, “Silica Sol-Gel/Organic Hybrid Material for Protein Encapsulated Column of Capillary Electrochromatography,” Journal of Chromatography A, Vol. 1044, No. 1-2, 2004, pp. 267-270. http://dx.doi.org/10.1016/j.chroma.2004.04.056 [18] M. Fujiwara, K. Shiokawa and T. Kubota, “Direct Encapsulation of Proteins into Calcium Silicate Microparticles by Water/Oil/Water Interfacial Reaction Method and Their Responsive Release Behaviors,” Materials Science and Engineering C, Vol. 32, No. 8, 2012, pp. 2484-2490. http://dx.doi.org/10.1016/j.msec.2012.07.030 [19] X. Y. Zhao, Y. J. Zhu, F. Chen and J. Wu, “Calcium Phosphate Nanocarriers Dual-Loaded with Bovine Serum Albumin and Ibuprofen: Facile Synthesis, Sequential Drug Loading and Sustained Drug Release,” Chemistry—An Asian Journal, Vol. 7, No. 7, 2012, pp. 1610-1615. http://dx.doi.org/10.1002/asia.201100954 [20] M. Igartua, R. M. Hernández, A. Esquisabel, A. R. Gascón, M. B. Calvo and J. L. Pedraz, “Stability of BSA Encapsulated into PLGA Microspheres Using PAGE and Capillary Electrophoresis,” International Journal of Pharmaceutics, Vol. 169, No. 1, 1998, pp. 45-54. http://dx.doi.org/10.1016/S0378-5173(98)00101-X [21] D. H. Chen, D. L. Cole and G. S. Srivatsa, “Determination of Free and Encapsulated Oligonucleotides in Liposome Formulated Drug Product,” Journal of Pharmaceutical and Biomedical Analysis, Vol. 22, No. 5, 2000, pp. 791-801. http://dx.doi.org/10.1016/S0731-7085(00)00243-0 [22] Tam. T. T. N. Nguyen, J. Ostergaard, S. Stürup and B. Gammelgaard, “Investigation of a Liposomal Oxaliplatin Drug Formulation by Capillary Electrophoresis Hyphenated to Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS),” Analytical and Bioanalytical Chemistry, Vol. 402, No. 6, 2012, pp. 2131-2139. http://dx.doi.org/10.1007/s00216-011-5651-6 [23] Tam. T. T. N. Nguyen, J. Ostergaard, S. Stürup and B. Gammelgaard, “Metallomics in Drug Development: Characterization of a Liposomal Cisplatin Drug Formulation in Human Plasma by CE-ICP-MS,” Analytical and Bioanalytical Chemistry, Vol. 405, No. 6, 2013, pp. 1845-1854. http://dx.doi.org/10.1007/s00216-012-6355-2 [24] K. J. Wiechelman, R. D. Braun and J. D. Fitzpatrick, “Investigation of the Bicinchoninic Acid Protein Assay: Identification of the Groups Responsible for Color Formation,” Analytical Biochemistry, Vol. 175, No. 1, 1988, pp. 231-237. http://dx.doi.org/10.1016/0003-2697(88)90383-1 [25] C. J. Brinker and G. W. Scherer, “Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing,” San Diego, CA, 1990. [26] J. J. Babcock and L. Brancaleon, “Bovine Serum Albumin Oligomers in the E-and B-Forms at Low Protein Concentration and Ionic Strength,” International Journal of Biological Macromolecules, Vol. 53, 2013, pp. 42-53. http://dx.doi.org/10.1016/j.ijbiomac.2012.10.030 [27] M. Dockal, D. C. Carter and F. Ruecker, “Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH,” The Journal of Biological Chemistry, Vol. 275, No. 5, 2000, pp. 3042-3050. http://dx.doi.org/10.1074/jbc.275.5.3042 [28] Y. F. Yan, D. Seeman, B. Q. Zheng, E. Kizilay, Y. S. Xu, and P. L. Dubin, “pH-Dependent Aggregation and Disaggregation of Native β-Lactoglobulin in Low Salt,” Langmuir, Vol. 29, No. 14, 2013, pp. 4584-4593. http://dx.doi.org/10.1021/la400258r [29] X. J. Gao, X. G. Zhang, X. J. Zhang, C. Cheng, Z. Wang and C. X. Li, “Encapsulation of BSA in Polylactic Acid-Hyperbranched Polyglycerol Conjugate Nanoparticles: Preparation, Characterization, and Release Kinetics,” Polymer Bulletin, Vol. 65, No. 8, 2010, pp. 787-805. http://dx.doi.org/10.1007/s00289-010-0273-2 [30] R. Viitala, M. Jokinen and J. B. Rosenholm, “Mechanistic Studies on Release of Large and Small Molecules from Biodegradable SiO2,” International Journal of Pharmaceutics, Vol. 336, No. 2, 2007, pp. 382-390. http://dx.doi.org/10.1016/j.ijpharm.2006.12.008 [31] C. Qi, Y. J. Zhu, B. Q. Lu, X. Y. Zhao, J. Zhao and F. Chen, “Hydroxyapatite Nanosheet-Assembled Porous Hollow Microspheres: DNA-Templated Hydrothermal Synthesis, Drug Delivery and Protein Adsorption,” Journal of Materials Chemistry, Vol. 22, No. 42, 2012, pp. 22642-22650. http://dx.doi.org/10.1039/C2JM35280J [32] M. Ahmed and R. Narain, “Intracellular Delivery of DNA and Enzyme in Active Form using Degradable Carbohydrate-Based Nanogels,” Molecular Pharmaceutics, Vol. 9, No. 11, 2012, pp. 3160-3170. http://dx.doi.org/10.1021/mp300255p
[1] R. Haag and F. Kratz, “Polymer Therapeutics: Concepts and Applications,” Angewandte Chemie, Vol. 45, No. 8, 2006, pp. 1198-1215. http://dx.doi.org/10.1002/anie.200502113 [2] M. Molinos, V. Carvalho, D. M. Silva and F. M. Gama, “Development of a Hybrid Dextrin Hydrogel Encapsulating Dextrin Nanogel as Protein Delivery System,” Biomacromolecules, Vol. 13, No. 2, 2012, pp. 517-527. http://dx.doi.org/10.1021/bm2015834 [3] G. J. Hickman, A. Rai, D. J. Boocock, R. C. Rees and C. C. Perry, “Fabrication, Characterisation and Performance of Hydrophilic and Superhydrophilic Silica as Cell Culture Surfaces,” Journal of Materials Chemistry, Vol. 22, No. 24, 2012, pp. 12141-12148. http://dx.doi.org/10.1039/c2jm31161e [4] M. R. N. Monton, E. M. Forsberg and J. D. Brennan, “Tailoring Sol-Gel-Derived Silica Materials for Optical Biosensing,” Chemistry of Materials, Vol. 24, No. 5, 2012, pp. 796-811. http://dx.doi.org/10.1021/cm202798e [5] W. Jin and J. D. Brennan, “Properties and Applications of Proteins Encapsulated within Sol-Gel Derived Materials,” Analytica Chimica Acta, Vol. 461, No. 1, 2002, pp. 1-36. http://dx.doi.org/10.1016/S0003-2670(02)00229-5 [6] I. Gill, “Bio-Doped Nanocomposite Polymers: Sol-Gel Bioencapsulates,” Chemistry of Materials, Vol. 13, No. 10, 2001, pp. 3404-3421. http://dx.doi.org/10.1021/cm0102483 [7] C. P. Liu and S. D. Liu, “Formulation and Characterization of the Microencapsulated Entomopathogenic Fungus Metarhizium anisopliae MA126,” Journal of Microencapsulation, Vol. 26, No. 5, 2009, pp. 377-384. http://dx.doi.org/10.1080/02652040802365455 [8] M. Kato, K. Inuzuka, K. Sakai-Kato and T. Toyo’oka, “Monolithic Bioreactor Immobilizing Trypsin for High-Throughput Analysis,” Analytical Chemistry, Vol. 77, No. 6, 2005, pp. 1813-1818. http://dx.doi.org/10.1021/ac048388u [9] S. Murayama, F. Ishizuka, K. Takagi, H. Inoda, A. Sano, T. Santa and M. Kato, “Small Mesh Size Hydrogel for Functional Photocontrol of Encapsulated Enzymes and Small Probe Molecules,” Analytical Chemistry, Vol. 84, No. 3, 2012, pp. 1374-1379. http://dx.doi.org/10.1021/ac2023603 [10] D. J. Dickson and R. L. Ely, “Silica Sol-Gel Encapsulation of Cyanobacteria: Lessons for Academic and Applied Research,” Applied Microbiology and Biotechnology, Vol. 97, No. 5, 2013, pp. 1809-1819. http://dx.doi.org/10.1007/s00253-012-4686-8 [11] N. Bhattarai, H. R. Ramay, J. Gunn, F. A. Matsen and M. Zhang, “PEG-Grafted Chitosan as an Injectable Thermosensitive Hydrogel for Sustained Protein Release,” Journal of Controlled Release, Vol. 103, No. 3, 2005, pp. 609-624. http://dx.doi.org/10.1016/j.jconrel.2004.12.019 [12] L. E. Vera-Avila, E. García-Salgado, M. P. García de Llasera and A. Pena-Alvarez, “Binding Characteristics of Bovine Serum Albumin Encapsulated in Sol-Gel Glasses: An Alternative for Protein Interaction Studies,” Analytical Biochemistry, Vol. 373, No. 2, 2008, pp. 272-280. http://dx.doi.org/10.1016/j.ab.2007.08.036 [13] C. D. Tran, D. Ilieva and S. Challa, “Inhomogeneity in Distribution and Conformation of Bovine Serum Albumin in Sol-Gel: A Closer Look with a Near-Infrared Multispectral Imaging Technique,” Journal of Sol-Gel Science and Technology, Vol. 32, No. 1-3, 2004, pp. 207-217. http://dx.doi.org/10.1007/s10971-004-5790-8 [14] Y. Gao, A. Heinemann, R. Knott and J. Bartlett, “Encapsulation of Protein in Silica Matrices: Structural Evolution on the Molecular and Nanoscales,” Langmuir, Vol. 26, No. 2, 2010, pp. 1239-1246. http://dx.doi.org/10.1021/la9023986 [15] M. Kato, K. Sakai-Kato, N. Matsumoto and T. Toyo’oka, “A Protein-Encapsulation Technique by the Sol-Gel Method for the Preparation of Monolithic Columns for Capillary Electrochromatography,” Analytical Chemistry, Vol. 74, No. 8, 2002, pp. 1915-1921. http://dx.doi.org/10.1021/ac0112162 [16] M. Kato, N. Matsumoto, K. Sakai-Kato and T. Toyo’oka, “Investigation of Chromatographic Performances and Binding Characteristics of BSA-Encapsulated Capillary Column Prepared by the Sol-Gel Method,” Journal of Pharmaceutical and Biomedical Analysis, Vol. 30, No. 6, 2003, pp. 1845-1850. http://dx.doi.org/10.1016/S0731-7085(02)00527-7 [17] M. Kato, H. Saruwatari, K. Sakai-Kato and T. Toyo’oka, “Silica Sol-Gel/Organic Hybrid Material for Protein Encapsulated Column of Capillary Electrochromatography,” Journal of Chromatography A, Vol. 1044, No. 1-2, 2004, pp. 267-270. http://dx.doi.org/10.1016/j.chroma.2004.04.056 [18] M. Fujiwara, K. Shiokawa and T. Kubota, “Direct Encapsulation of Proteins into Calcium Silicate Microparticles by Water/Oil/Water Interfacial Reaction Method and Their Responsive Release Behaviors,” Materials Science and Engineering C, Vol. 32, No. 8, 2012, pp. 2484-2490. http://dx.doi.org/10.1016/j.msec.2012.07.030 [19] X. Y. Zhao, Y. J. Zhu, F. Chen and J. Wu, “Calcium Phosphate Nanocarriers Dual-Loaded with Bovine Serum Albumin and Ibuprofen: Facile Synthesis, Sequential Drug Loading and Sustained Drug Release,” Chemistry—An Asian Journal, Vol. 7, No. 7, 2012, pp. 1610-1615. http://dx.doi.org/10.1002/asia.201100954 [20] M. Igartua, R. M. Hernández, A. Esquisabel, A. R. Gascón, M. B. Calvo and J. L. Pedraz, “Stability of BSA Encapsulated into PLGA Microspheres Using PAGE and Capillary Electrophoresis,” International Journal of Pharmaceutics, Vol. 169, No. 1, 1998, pp. 45-54. http://dx.doi.org/10.1016/S0378-5173(98)00101-X [21] D. H. Chen, D. L. Cole and G. S. Srivatsa, “Determination of Free and Encapsulated Oligonucleotides in Liposome Formulated Drug Product,” Journal of Pharmaceutical and Biomedical Analysis, Vol. 22, No. 5, 2000, pp. 791-801. http://dx.doi.org/10.1016/S0731-7085(00)00243-0 [22] Tam. T. T. N. Nguyen, J. Ostergaard, S. Stürup and B. Gammelgaard, “Investigation of a Liposomal Oxaliplatin Drug Formulation by Capillary Electrophoresis Hyphenated to Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS),” Analytical and Bioanalytical Chemistry, Vol. 402, No. 6, 2012, pp. 2131-2139. http://dx.doi.org/10.1007/s00216-011-5651-6 [23] Tam. T. T. N. Nguyen, J. Ostergaard, S. Stürup and B. Gammelgaard, “Metallomics in Drug Development: Characterization of a Liposomal Cisplatin Drug Formulation in Human Plasma by CE-ICP-MS,” Analytical and Bioanalytical Chemistry, Vol. 405, No. 6, 2013, pp. 1845-1854. http://dx.doi.org/10.1007/s00216-012-6355-2 [24] K. J. Wiechelman, R. D. Braun and J. D. Fitzpatrick, “Investigation of the Bicinchoninic Acid Protein Assay: Identification of the Groups Responsible for Color Formation,” Analytical Biochemistry, Vol. 175, No. 1, 1988, pp. 231-237. http://dx.doi.org/10.1016/0003-2697(88)90383-1 [25] C. J. Brinker and G. W. Scherer, “Sol-Gel Science: The Physics and Chemistry of Sol-Gel Processing,” San Diego, CA, 1990. [26] J. J. Babcock and L. Brancaleon, “Bovine Serum Albumin Oligomers in the E-and B-Forms at Low Protein Concentration and Ionic Strength,” International Journal of Biological Macromolecules, Vol. 53, 2013, pp. 42-53. http://dx.doi.org/10.1016/j.ijbiomac.2012.10.030 [27] M. Dockal, D. C. Carter and F. Ruecker, “Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH,” The Journal of Biological Chemistry, Vol. 275, No. 5, 2000, pp. 3042-3050. http://dx.doi.org/10.1074/jbc.275.5.3042 [28] Y. F. Yan, D. Seeman, B. Q. Zheng, E. Kizilay, Y. S. Xu, and P. L. Dubin, “pH-Dependent Aggregation and Disaggregation of Native β-Lactoglobulin in Low Salt,” Langmuir, Vol. 29, No. 14, 2013, pp. 4584-4593. http://dx.doi.org/10.1021/la400258r [29] X. J. Gao, X. G. Zhang, X. J. Zhang, C. Cheng, Z. Wang and C. X. Li, “Encapsulation of BSA in Polylactic Acid-Hyperbranched Polyglycerol Conjugate Nanoparticles: Preparation, Characterization, and Release Kinetics,” Polymer Bulletin, Vol. 65, No. 8, 2010, pp. 787-805. http://dx.doi.org/10.1007/s00289-010-0273-2 [30] R. Viitala, M. Jokinen and J. B. Rosenholm, “Mechanistic Studies on Release of Large and Small Molecules from Biodegradable SiO2,” International Journal of Pharmaceutics, Vol. 336, No. 2, 2007, pp. 382-390. http://dx.doi.org/10.1016/j.ijpharm.2006.12.008 [31] C. Qi, Y. J. Zhu, B. Q. Lu, X. Y. Zhao, J. Zhao and F. Chen, “Hydroxyapatite Nanosheet-Assembled Porous Hollow Microspheres: DNA-Templated Hydrothermal Synthesis, Drug Delivery and Protein Adsorption,” Journal of Materials Chemistry, Vol. 22, No. 42, 2012, pp. 22642-22650. http://dx.doi.org/10.1039/C2JM35280J [32] M. Ahmed and R. Narain, “Intracellular Delivery of DNA and Enzyme in Active Form using Degradable Carbohydrate-Based Nanogels,” Molecular Pharmaceutics, Vol. 9, No. 11, 2012, pp. 3160-3170. http://dx.doi.org/10.1021/mp300255p