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　　References:

　　1. Vaillard, V.A., et al., mPEG–NHS carbonates: Effect of alkyl spacers on the reactivity: Kinetic and mechanistic insights, Journal of Applied Polymer Science, 2019, 136(5):47028.

　　2. Ma, S.S., et al., The pharmacokinetic and pharmacodynamic properties of site-specific pegylated genetically modified recombinant human interleukin-11 in normal and thrombocytopenic monkeys, European Journal of Pharmaceutics and Biopharmaceutics, 2017.

　　3. Zhao, Y.Z., et al., PEGylation with the thiosuccinimido butylamine linker significantly increases the stability of haloalkane dehalogenase DhaA, Journal of Biotechnology, 2017.

　　4. Lee, K., et al., Enhanced accumulation of theranostic nanoparticles in brain tumor by external magnetic field mediated in situ clustering of magnetic nanoparticles, Journal of Industrial and Engineering Chemistry, 2017.

　　5. Wan, X., et al., Effect of protein immunogenicity and PEG size and branching on the anti-PEG immune response to PEGylated proteins, Process Biochemistry, 2017, 52:183-91.

　　6. Fahrlander E., et al., PEGylated human serum albumin (HSA) nanoparticles: preparation, characterization and quantification of the PEGylation extent, Nanotechnology, 2015, 26(14):145103.

　　7. Zhang, J., et al., Magnetic Targeting of Novel Heparinized Iron Oxide Nanoparticles Evaluated in a 9L-glioma Mouse Model, Pharmaceutical Research, 2014, 31:3, pp 579-592.

　　8. Peng, F., et al., PEGylation of G-CSF in organic solvent markedly increase the efficacy and reactivity through protein unfolding, hydrolysis inhibition and solvent effect. Journal of Biotechnology, 2014, 170: p. 42-49.

　　9. Mingji Jin, et al, Preparation of pegylated lumbrokinase and an evaluation of its thrombolytic activity both in vitro and in vivo, Acta Pharmaceutica Sinica B, 2013, 3(2) p: 123-129.

　　10. Zhang, J., et al., Long-Circulating Heparin-Functionalized Magnetic Nanoparticles for Potential Application as a Protein Drug Delivery Platform, Molecular Pharmaceutics, 2013, 10(10), 3892-3902.

　　11. Jun Wang, et al., An oriented adsorption strategy for efficient solid phase PEGylation of recombinant staphylokinase by immobilized metal-ion affinity chromatography, Process Biochemistry, 2012, 47, 1, p: 106-112.

　　12. Liu, S.. et al., Mono-PEGylation of ribonuclease A: High PEGylation efficiency by thiolation with small molecular weight reagent, Process Biochemistry, 2012, 47(9), p: 1364-1370.

　　13. Peng, F., et al., PEGylation of Proteins in Organic Solution: A Case Study for Interferon beta-1b, Bioconjugate Chem., 2012, 23 (9), 1812-1820.

　　14. Beibei, H., Design, Preparation and in vitro Bioactivity of Mono-PEGylated Recombinant Hirudin, Chin. J. Chem. Eng., 2007, 15(6) 775—780.

15.Ren, M., et al., An oligopeptide/aptamer-conjugated dendrimer-based nanocarrier for dual-targeting delivery to bone. Journal of Materials Chemistry B. 2021, 9(12):2831-44.