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This work is licensed under a Creative Commons Attribution 4.0 International License.
Protein Immobilization on A Biotinylated Polymer Coating
Corresponding Author(s) : Xiaohong Zhang
Asian Journal of Chemistry,
Vol. 25 No. 2 (2013): Vol 25 Issue 2
Abstract
A polymer coating to specifically immobilize proteins was constructed from a biodegradable amphiphilic triblock copolymer, biotinylated poly(ethylene glycol)-b-poly(L-lactide)-b-poly(Llysine) (PEG-PLA-PLL/biotin), accompanied by covering it with a layer of blocking agent consisting of gelatin, poly(N-vinyl pyrrolidone) and casein. The bioactive surface was characterized by a confocal laser scanning microscope analysis by means of consecutive immobilization of non-labeled streptavidin, biotinylated rabbit antigoat monoclonal antibodies and FITC-labeled goat globulin. In results, the bioactive surface repelled nonspecific protein and allowed specific biotin-streptavidin interaction; meanwhile the immobilized streptavidin kept its bioactivity. In addition, the PEG-PLA-PLL/biotin coating could enhance the attachment and proliferation of mouse L929 fibroblasts, suggesting that it had excellent biocompatibility. The PEG-PLA-PLL/biotin is potential to become a bioactive material for protein immobilization and biodegradable scaffolds.
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- N.-P. Huang, J. Vörös, S.M. DePaul, M. Textor and N.D. Spencer, Langmuir, 18, 220 (2002).
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References
N.-P. Huang, J. Vörös, S.M. DePaul, M. Textor and N.D. Spencer, Langmuir, 18, 220 (2002).
J.G. Groll, E.V. Amirgoulova, T. Ameringer, C.D. Heyes, C. Rocker, G.U. Nienhaus and M. Moller, J. Am. Chem. Soc., 126, 4234 (2004).
G.W. Fussell and S.L. Cooper, Biomaterials, 25, 2971 (2004).
Z. Zhang, S.F. Chen and S.Y. Jiang, Biomacromolecules, 7, 3311 (2006).
S. Ko and J. Jang, Biomacromolecules, 8, 1400 (2008).
S. Tosatti, R. Michel, M. Texxtor and N.D. Spencer, Langmuir, 18, 3537 (2002).
K.Y. Lee and D.J. Mooney, Chem. Rev., 101, 1869 (2001).
K. Huang, B.P. Lee, D.R. Ingram and P.D. Messersmith, Biomacromolecules, 3, 397 (2002).
D. Anderheiden, O. Brenner, D. Klee, R. Kaufmann, H.A. Richter, P.T Bury and R. Langer, J. Am. Chem. Soc., 115, 11010 (1993).
C. Rosano, P. Arioso and M. Bolognesl, Biomol. Eng., 16, 5 (1999).
N.M. Green, Avidin, in Advances in Protein Chemistry, Academic Press, New York, Vol. 29, pp. 85-133 (1975).
C. Deng, X. Chen, H. Yu, J. Sun, T. Lu and X. Jing, Polymer, 48, 139 (2007).
M. Wilchek and E.A. Bayer, Methods Enzymol., 184, 123 (1990).
W.M. Huang, S.J. Gibson, P. Facer, J. Gu and J.M. Polak, Histochem., 77, 275 (1983).
D. Li, M.W. Frey and A.J. Baeumnerb, J. Membr. Sci., 279, 354 (2006).
F. Bibbs, ELISA Technical Bulletin-No. 3, Corning Life Sciences, Kennebunk, ME, USA, Retrieved web site, http://www.corning.com/lifesciences
R.F. Vogt, D.L. Phillips Jr., L. Omar Henderson, W. Whitfield and F.W. Spierto, J. Immunol. Methods, 101, 43 (1987).
S.C. Lakhotia, A. Sharma, M. Mutsuddi and M.G. Tapadia, Trends Genet., 9, 261 (1993).
T. Lu, C. Deng, J. Sun, X. Chen, P. Zhang and X. Jing, Chem. J. Chin. Univ., 29, 837 (2008).
F. Rusmini, Z. Zhong and J. Feijen, Biomacromolecules, 8, 1775 (2007).
M. González, C. Argarana and G.D. Fidelio, Biomol. Eng., 16, 67 (1999).