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Issue 10, 2013
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Controlled release of human growth hormone fused with a human hybrid Fc fragment through a nanoporous polymer membrane

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Abstract

Nanotechnology has been applied to the development of more effective and compatible drug delivery systems for therapeutic proteins. Human growth hormone (hGH) was fused with a hybrid Fc fragment containing partial Fc domains of human IgD and IgG4 to produce a long-acting fusion protein. The fusion protein, hGH-hyFc, resulted in the increase of the hydrodynamic diameter (ca. 11 nm) compared with the diameter (ca. 5 nm) of the recombinant hGH. A diblock copolymer membrane with nanopores (average diameter of 14.3 nm) exhibited a constant release rate of hGH-hyFc. The hGH-hyFc protein released in a controlled manner for one month was found to trigger the phosphorylation of Janus kinase 2 (JAK2) in human B lymphocyte and to exhibit an almost identical circular dichroism spectrum to that of the original hGH-hyFc, suggesting that the released fusion protein should maintain the functional and structural integrity of hGH. Thus, the nanoporous release device could be a potential delivery system for the long-term controlled release of therapeutic proteins fused with the hybrid Fc fragment.

Graphical abstract: Controlled release of human growth hormone fused with a human hybrid Fc fragment through a nanoporous polymer membrane

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Publication details

The article was received on 27 Jan 2013, accepted on 07 Mar 2013 and first published on 12 Mar 2013


Article type: Paper
DOI: 10.1039/C3NR00474K
Citation: Nanoscale, 2013,5, 4262-4269
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    Controlled release of human growth hormone fused with a human hybrid Fc fragment through a nanoporous polymer membrane

    E. Kim, D. S. Jang, S. Y. Yang, M. N. Lee, K. S. Jin, H. J. Cha, J. K. Kim, Y. C. Sung and K. Y. Choi, Nanoscale, 2013, 5, 4262
    DOI: 10.1039/C3NR00474K

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