Biology:Glycopegylation
From HandWiki
Glycopegylation "is a site-selective PEGylation method developed for modifying complex glycoproteins".[1] It can be useful to improve bioavailability and extend the half-life of various therapeutic proteins.[2][1][3] Examples of glycopegylated molecules include pegozafermin[4] and recombinant factor IX.[5]
References
- ↑ 1.0 1.1 Behrens, Carsten; Buchardt, Jens (1 January 2020). "12 - Sialyltransferase-mediated glycoPEGylation". Polymer-Protein Conjugates. Elsevier. pp. 251–269. ISBN 978-0-444-64081-9. https://www.sciencedirect.com/science/article/abs/pii/B9780444640819000127.
- ↑ Abdolzade-Bavil, Afsaneh; Cooksey, Bridget A.; Scheckermann, Christian; Lammerich, Andreas; Pukac, Laurie; Krasney, Philip; Allgaier, Hermann; Shen, Wenyan David et al. (15 November 2013). "Pegylated Versus Glycopegylated G-CSFs and Their Biochemical and Physiological Properties". Blood 122 (21): 4851. doi:10.1182/blood.V122.21.4851.4851.
- ↑ DeFrees, Shawn; Wang, Zhi-Guang; Xing, Ruye; Scott, Arthur E.; Wang, Jin; Zopf, David; Gouty, Dominique L.; Sjoberg, Eric R. et al. (1 September 2006). "GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli". Glycobiology 16 (9): 833–843. doi:10.1093/glycob/cwl004. PMID 16717104.
- ↑ Loomba, Rohit; Sanyal, Arun J.; Kowdley, Kris V.; Bhatt, Deepak L.; Alkhouri, Naim; Frias, Juan P.; Bedossa, Pierre; Harrison, Stephen A. et al. (14 September 2023). "Randomized, Controlled Trial of the FGF21 Analogue Pegozafermin in NASH". New England Journal of Medicine 389 (11): 998–1008. doi:10.1056/NEJMoa2304286. PMID 37356033.
- ↑ Nielsen, Finn Stausholm; Schmidt, Anette Skammelsen; Kristensen, Anne Kroll; Nielsen, Anders Dybdal; Kristensen, Brian Kåre; Palm, Lisbeth (October 2020). "Characterisation of recombinant factor IX before and after GlycoPEGylation". International Journal of Pharmaceutics 588: 119654. doi:10.1016/j.ijpharm.2020.119654. PMID 32693290.
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