Hostname: page-component-586b7cd67f-g8jcs Total loading time: 0 Render date: 2024-11-28T13:05:16.967Z Has data issue: false hasContentIssue false
  • English
  • Français

Encapsulation of Stimuli-Responsive Fusion Proteins in Silica: Thermally Responsive Metal Ion-Sensitive Hybrid Membranes

Published online by Cambridge University Press:  11 March 2013

Linying Li ,
Owen Im ,
Ashutosh Chilkoti  and
Gabriel P. López
Linying Li
Affiliation:
Department of Biomedical Engineering, Duke University, Durham NC 27708, U.S.A. NSF Research Triangle Materials Research Science and Engineering Center, U.S.A
Owen Im
Affiliation:
Department of Biomedical Engineering, Duke University, Durham NC 27708, U.S.A.
Ashutosh Chilkoti
Affiliation:
Department of Biomedical Engineering, Duke University, Durham NC 27708, U.S.A. Department of Mechanical Engineering and Materials Science, Duke University, Durham NC 27708, U.S.A. NSF Research Triangle Materials Research Science and Engineering Center, U.S.A
Gabriel P. López
Affiliation:
Department of Biomedical Engineering, Duke University, Durham NC 27708, U.S.A. Department of Mechanical Engineering and Materials Science, Duke University, Durham NC 27708, U.S.A. NSF Research Triangle Materials Research Science and Engineering Center, U.S.A
Get access

Abstract

In this study, we demonstrate the fabrication of hybrid membranes that exhibit discrete and reversible changes in permeability in response to changes in calcium ion (Ca2+) concentration and temperature. Fusion proteins comprising calmodulin (CAM) and elastin-like polypeptides (ELPs) were used as stimuli-responsive elements due to their ability to undergo a reversible lower critical solution temperature (LCST) phase transition, which is sensitive to Ca2+ binding. The calmodulin elastin-like polypeptides fusions (CAM-ELPs) were incorporated into polymerizing silica networks using a simple sol-gel process and spin coating. Permeation experiments with solutions of crystal violet showed that the membranes are both Ca2+-responsive and thermally responsive. Under suitable pressure drop across the membranes, in the absence of Ca2+ or below the LCST of the ELPs, the hybrid membranes are impermeable to water. After addition of Ca2+ or above the LCSTs, they become permeable to water. The permeability can be toggled back and forth by sequential addition of calcium and ethylenediamine tetraacetic acid (EDTA). These results demonstrate that CAMELP/silica hybrid membranes can serve as tunable molecular filters whose permeability can be switched on and off in response to Ca2+ and temperature.

Keywords

biomaterialsol-gelthin film
Type
Articles
Information
MRS Online Proceedings Library (OPL) , Volume 1498: Symposium M – Biomimetic, Bio-inspired and Self-Assembled Materials for Engineered Surfaces and Applications , 2013 , pp. 169 - 175
Copyright
Copyright © Materials Research Society 2013 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Mendes, P. M., Chem. Soc. Rev., 37, 2512 (2008).CrossRefGoogle Scholar
Banki, M. R., Feng, L., Wood, D.W., Nature Methods, 2, 659–662 (2005).CrossRefGoogle Scholar
Xu, C., Wayland, B. B., Fryd, M., Winey, K. I., and Composto, R. J., Macromolecules, 39, 6063 (2006).CrossRefGoogle Scholar
Alexandridis, P., Lindman, B., Amphiphilic Block Copolymers: Self-Assembly and Applications, 1 st ed. (Elsevier Science, Netherlands, 2000)Google Scholar
Chilkoti, A., Dreher, M.R., Meyer, D.E., Raucher, D., Advanced Drug Delivery Reviews, 5,613–630 (2002).CrossRefGoogle Scholar
Urry, D. W., J. Phys. Chem. B, 101, 11007–11028 (1997).CrossRefGoogle Scholar
Urry, D. W., Angew. Chem. Int. Ed., 32, 819 (2003).CrossRefGoogle Scholar
Carlson, K. T., Meyer, D. E., and Liu, L., Peds. 17,1 (2004).Google Scholar
Meyer, D. E., Carlson, K. T., Chilkoti, A., Biotechnol. Prog 17, 720 (2001).CrossRefGoogle Scholar
Carlson, K. T., Liu, L., Kim, B., Chilkoti, A., Protein Science, 13,12 (2004).Google Scholar
Kim, B. and Chilkoti, A., Journal of the American Chemical Society, 130, 17867 (2008).CrossRefGoogle Scholar
Banta, S., Wheeldon, I. R., and Blenner, M., Annu. Rev. Biomed. Eng., 12, 167 (2010).CrossRefGoogle Scholar
Girotti, A., Reguera, J., and Rodríguez-Cabello, J. C., J Mater Sci Mater Med, 15, 479 (2004).CrossRefGoogle Scholar
Morrow, C., Minehan, D. S., Wu, J., and Hunter, E., Biotechnol Prog, 8, 347 (1992).Google Scholar
Meyer, D. E. and Chilkoti, A. A. Biomacromolecules, 3, 357–367 (2002).CrossRefGoogle Scholar
Fu, Q., Rao, G. V. R., Ista, L. K., Wu, Y., Andrzejewski, B. P., Sklar, L. A., Ward, T. L., and Lopez, G. P., Advanced Materials, 15, 1262 (2003).CrossRefGoogle Scholar
Rao, G. V. R., Balamurugan, S., Meyer, D. E., Chilkoti, A., and Lopez, G. P., Langmuir, 18, 1819 (2002).CrossRefGoogle Scholar