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Journal of Drug Delivery
Volume 2016, Article ID 7843951, 9 pages
http://dx.doi.org/10.1155/2016/7843951
Research Article

PEG-Immobilized Keratin for Protein Drug Sequestration and pH-Mediated Delivery

Bioengineering Program, Department of Engineering, Hofstra University, Hempstead, NY 11549, USA

Received 11 September 2015; Revised 23 December 2015; Accepted 27 December 2015

Academic Editor: Subbu S. Venkatraman

Copyright © 2016 Roche C. de Guzman and Sina Y. Rabbany. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. K. Karathanasis, “Regenerative medicine: transforming the drug discovery and development paradigm,” Cold Spring Harbor Perspectives in Medicine, vol. 4, no. 8, Article ID a014084, 2014. View at Publisher · View at Google Scholar
  2. S. Barrientos, H. Brem, O. Stojadinovic, and M. Tomic-Canic, “Clinical application of growth factors and cytokines in wound healing,” Wound Repair and Regeneration, vol. 22, no. 5, pp. 569–578, 2014. View at Publisher · View at Google Scholar
  3. P. Koria, “Delivery of growth factors for tissue regeneration and wound healing,” BioDrugs, vol. 26, no. 3, pp. 163–175, 2012. View at Publisher · View at Google Scholar · View at Scopus
  4. K. Lee, E. A. Silva, and D. J. Mooney, “Growth factor delivery-based tissue engineering: general approaches and a review of recent developments,” Journal of the Royal Society Interface, vol. 8, no. 55, pp. 153–170, 2011. View at Publisher · View at Google Scholar · View at Scopus
  5. B. Alberts, Molecular Biology of the Cell, Garland Science, New York, NY, USA, 5th edition, 2008.
  6. K. Vulic and M. S. Shoichet, “Affinity-based drug delivery systems for tissue repair and regeneration,” Biomacromolecules, vol. 15, no. 11, pp. 3867–3880, 2014. View at Publisher · View at Google Scholar · View at Scopus
  7. G. Gainza, S. Villullas, J. L. Pedraz, R. M. Hernandez, and M. Igartua, “Advances in drug delivery systems (DDSs) to release growth factors for wound healing and skin regeneration,” Nanomedicine, vol. 11, no. 6, pp. 1551–1573, 2015. View at Publisher · View at Google Scholar
  8. Y. Liang and K. L. Kiick, “Heparin-functionalized polymeric biomaterials in tissue engineering and drug delivery applications,” Acta Biomaterialia, vol. 10, no. 4, pp. 1588–1600, 2014. View at Publisher · View at Google Scholar · View at Scopus
  9. F. M. A. H. Schuurmans Stekhoven, M. H. A. G. Gorissen, and G. Flik, “The isoelectric point, a key to understanding a variety of biochemical problems: a minireview,” Fish Physiology and Biochemistry, vol. 34, no. 1, pp. 1–8, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. A. Wittemann and M. Ballauff, “Interaction of proteins with linear polyelectrolytes and spherical polyelectrolyte brushes in aqueous solution,” Physical Chemistry Chemical Physics, vol. 8, no. 45, pp. 5269–5275, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. K. Knop, R. Hoogenboom, D. Fischer, and U. S. Schubert, “Poly(ethylene glycol) in drug delivery: pros and cons as well as potential alternatives,” Angewandte Chemie—International Edition, vol. 49, no. 36, pp. 6288–6308, 2010. View at Publisher · View at Google Scholar · View at Scopus
  12. B. Engebretson and V. I. Sikavitsas, “Long-term in vivo effect of peg bone tissue engineering scaffolds,” Journal of Long-Term Effects of Medical Implants, vol. 22, no. 3, pp. 211–218, 2012. View at Publisher · View at Google Scholar · View at Scopus
  13. G. M. Bonora and S. Drioli, “Recent advances on patents in poly(ethylene glycol)-based drug delivery,” Recent Patents on Drug Delivery and Formulation, vol. 2, no. 2, pp. 189–195, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Kolate, D. Baradia, S. Patil, I. Vhora, G. Kore, and A. Misra, “PEG—a versatile conjugating ligand for drugs and drug delivery systems,” Journal of Controlled Release, vol. 192, pp. 67–81, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. J. K. Tessmar and A. M. Göpferich, “Customized PEG-derived copolymers for tissue-engineering applications,” Macromolecular Bioscience, vol. 7, no. 1, pp. 23–39, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. H. Takahashi, Y. Wang, and D. W. Grainger, “Device-based local delivery of siRNA against mammalian target of rapamycin (mTOR) in a murine subcutaneous implant model to inhibit fibrous encapsulation,” Journal of Controlled Release, vol. 147, no. 3, pp. 400–407, 2010. View at Publisher · View at Google Scholar · View at Scopus
  17. G. D. Mogoşanu, A. M. Grumezescu, and M. C. Chifiriuc, “Keratin-based biomaterials for biomedical applications,” Current Drug Targets, vol. 15, no. 5, pp. 518–530, 2014. View at Publisher · View at Google Scholar · View at Scopus
  18. P. Hill, H. Brantley, and M. Van Dyke, “Some properties of keratin biomaterials: kerateines,” Biomaterials, vol. 31, no. 4, pp. 585–593, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Vasconcelos and A. Cavaco-Paulo, “The use of keratin in biomedical applications,” Current Drug Targets, vol. 14, no. 5, pp. 612–619, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. K. T. Nguyen and J. L. West, “Photopolymerizable hydrogels for tissue engineering applications,” Biomaterials, vol. 23, no. 22, pp. 4307–4314, 2002. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Sokic, M. Christenson, J. Larson, and G. Papavasiliou, “In situ generation of cell-laden porous MMP-sensitive PEGDA hydrogels by gelatin leaching,” Macromolecular Bioscience, vol. 14, no. 5, pp. 731–739, 2014. View at Publisher · View at Google Scholar · View at Scopus
  22. R. C. de Guzman, S. M. Tsuda, M.-T. N. Ton et al., “Binding interactions of keratin-based hair fiber extract to gold, keratin, and BMP-2,” PLoS ONE, vol. 10, no. 8, Article ID e0137233, 2015. View at Publisher · View at Google Scholar
  23. J. R. Richter, R. C. de Guzman, O. K. Greengauz-Roberts, and M. Van Dyke, “Structure-property relationships of meta-kerateine biomaterials derived from human hair,” Acta Biomaterialia, vol. 8, no. 1, pp. 274–281, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. K. Xu, Y. Fu, W. Chung et al., “Thiol-ene-based biological/synthetic hybrid biomatrix for 3-D living cell culture,” Acta Biomaterialia, vol. 8, no. 7, pp. 2504–2516, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. C.-C. Lin, A. Raza, and H. Shih, “PEG hydrogels formed by thiol-ene photo-click chemistry and their effect on the formation and recovery of insulin-secreting cell spheroids,” Biomaterials, vol. 32, no. 36, pp. 9685–9695, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. V. Joukov, K. Pajusola, A. Kaipainen et al., “A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases,” The EMBO Journal, vol. 15, no. 2, pp. 290–298, 1996. View at Google Scholar · View at Scopus
  27. T. Klaus, M. Kulesza, M. Bzowska, B. Wyroba, W. W. Kilarski, and J. Bereta, “Overcoming inefficient secretion of recombinant VEGF-C in baculovirus expression vector system by simple purification of the protein from cell lysate,” Protein Expression and Purification, vol. 110, pp. 151–158, 2015. View at Publisher · View at Google Scholar
  28. R. Pethig, “Dielectric properties of biological materials: biophysical and medical applications,” IEEE Transactions on Electrical Insulation, vol. 19, no. 5, pp. 453–474, 1984. View at Publisher · View at Google Scholar · View at Scopus
  29. V. M. Hernandez-Izquierdo and J. M. Krochta, “Thermoplastic processing of proteins for film formation—a review,” Journal of Food Science, vol. 73, no. 2, pp. R30–R39, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. J. H. Lee and D. G. Bucknall, “Swelling behavior and network structure of hydrogels synthesized using controlled UV-initiated free radical polymerization,” Journal of Polymer Science Part B: Polymer Physics, vol. 46, no. 14, pp. 1450–1462, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. S. J. Bryant and K. S. Anseth, “Photopolymerization of hydrogel scaffolds,” in Scaffolding in Tissue Engineering, P. X. Ma and J. H. Elisseeff, Eds., pp. 71–90, Taylor & Francis, Boca Raton, Fla, USA, 2006. View at Google Scholar
  32. A.-A. A. Abdel-Azim, A. M. Abdul-Raheim, A. M. Atta, W. Brostow, and T. Datashvili, “Swelling and network parameters of crosslinked porous octadecyl acrylate copolymers as oil spill sorbers,” e-Polymers, vol. 9, no. 1, pp. 1592–1605, 2009. View at Google Scholar
  33. G. Colucci, A. Aluigi, C. Tonin, and R. Bongiovanni, “Photopolymerization of keratin-based thiol-ene coatings,” Progress in Organic Coatings, vol. 77, no. 6, pp. 1104–1110, 2014. View at Publisher · View at Google Scholar · View at Scopus
  34. T. M. Florence, “Degradation of protein disulphide bonds in dilute alkali,” Biochemical Journal, vol. 189, no. 3, pp. 507–520, 1980. View at Publisher · View at Google Scholar · View at Scopus
  35. J. E. Glasgow, M. A. Asensio, C. M. Jakobson, M. B. Francis, and D. Tullman-Ercek, “Influence of electrostatics on small molecule flux through a protein nanoreactor,” ACS Synthetic Biology, vol. 4, no. 9, pp. 1011–1019, 2015. View at Publisher · View at Google Scholar
  36. D. V. Volodkin, N. I. Larionova, and G. B. Sukhorukov, “Protein encapsulation via porous CaCO3 microparticles templating,” Biomacromolecules, vol. 5, no. 5, pp. 1962–1972, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. K. M. Bernot, C.-H. Lee, and P. A. Coulombe, “A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability,” Journal of Cell Biology, vol. 168, no. 6, pp. 965–974, 2005. View at Publisher · View at Google Scholar · View at Scopus
  38. U. Kragh-Hansen, “Structure and ligand binding properties of human serum albumin,” Danish Medical Bulletin, vol. 37, no. 1, pp. 57–84, 1990. View at Google Scholar · View at Scopus
  39. K. Andreas, M. Sittinger, and J. Ringe, “Toward in situ tissue engineering: chemokine-guided stem cell recruitment,” Trends in Biotechnology, vol. 32, no. 9, pp. 483–492, 2014. View at Publisher · View at Google Scholar · View at Scopus
  40. S. Reed and B. Wu, “Sustained growth factor delivery in tissue engineering applications,” Annals of Biomedical Engineering, vol. 42, no. 7, pp. 1528–1536, 2014. View at Publisher · View at Google Scholar · View at Scopus
  41. H. Uludag, W. Friess, D. Williams et al., “rhBMP-collagen sponges as osteoinductive devices: effects of in vitro sponge characteristics and protein pI on in vivo rhBMP pharmacokinetics,” Annals of the New York Academy of Sciences, vol. 875, pp. 369–378, 1999. View at Publisher · View at Google Scholar · View at Scopus
  42. J. M. Wozney, V. Rosen, A. J. Celeste et al., “Novel regulators of bone formation: molecular clones and activities,” Science, vol. 242, no. 4885, pp. 1528–1534, 1988. View at Publisher · View at Google Scholar · View at Scopus
  43. A. L. Mandel, H. Ozdener, and V. Utermohlen, “Identification of pro- and mature brain-derived neurotrophic factor in human saliva,” Archives of Oral Biology, vol. 54, no. 7, pp. 689–695, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. J. R. Richter, R. C. de Guzman, and M. E. Van Dyke, “Mechanisms of hepatocyte attachment to keratin biomaterials,” Biomaterials, vol. 32, no. 30, pp. 7555–7561, 2011. View at Publisher · View at Google Scholar · View at Scopus
  45. H. Y. Shin, M. L. Smith, K. J. Toy, P. M. Williams, R. Bizios, and M. E. Gerritsen, “VEGF-C mediates cyclic pressure-induced endothelial cell proliferation,” Physiological Genomics, vol. 11, no. 3, pp. 245–251, 2002. View at Google Scholar · View at Scopus
  46. J. W. Breslin, S. Y. Yuan, and M. H. Wu, “VEGF-C alters barrier function of cultured lymphatic endothelial cells through a VEGFR-3-dependent mechanism,” Lymphatic Research and Biology, vol. 5, no. 2, pp. 105–113, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. H. Shimoda and S. Kato, “A model for lymphatic regeneration in tissue repair of the intestinal muscle coat,” International Review of Cytology, vol. 250, pp. 73–108, 2006. View at Publisher · View at Google Scholar · View at Scopus
  48. A. Yan, T. Avraham, J. C. Zampell, S. Z. Aschen, and B. J. Mehrara, “Mechanisms of lymphatic regeneration after tissue transfer,” PLoS ONE, vol. 6, no. 2, Article ID e17201, 2011. View at Publisher · View at Google Scholar · View at Scopus
  49. H. W. Schnaper, H. K. Kleinman, and D. S. Grant, “Role of laminin in endothelial cell recognition and differentiation,” Kidney International, vol. 43, no. 1, pp. 20–25, 1993. View at Publisher · View at Google Scholar · View at Scopus