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Issue 9, 2012
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PEG-urokinase nanogels with enhanced stability and controllable bioactivity

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Abstract

Protein nanogels were synthesized via a one-step reaction procedure by crosslinking urokinase with benzaldehyde bifunctionalized poly(ethylene glycol). The crosslinked architecture significantly enhances the stability of urokinase against enzyme degradation in comparison with the core–shell structural PEGylated proteins. Meanwhile, bioactivity of the urokinase incorporated in the nanogels can be adjusted by varying the chain length of the corsslinking polymer. With a shorter crosslinker the bioactivity of the uPA nanogels is seriously restricted under physiological conditions. However, the restricted bioactivity can be completely launched by either enlarging the mesh size of the nanogel by using longer crosslinkers, or treating the nanogels in endosomal conditions to dissociate the nanogel structure due to the reversible conjugation chemistry.

Graphical abstract: PEG-urokinase nanogels with enhanced stability and controllable bioactivity

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Publication details

The article was received on 31 Oct 2011, accepted on 05 Dec 2011 and first published on 23 Jan 2012


Article type: Paper
DOI: 10.1039/C2SM07072C
Citation: Soft Matter, 2012,8, 2644-2650
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    PEG-urokinase nanogels with enhanced stability and controllable bioactivity

    H. Tan, H. Jin, H. Mei, L. Zhu, W. Wei, Q. Wang, F. Liang, C. Zhang, J. Li, X. Qu, D. Shangguan, Y. Huang and Z. Yang, Soft Matter, 2012, 8, 2644
    DOI: 10.1039/C2SM07072C

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