Biomaterials 2014 Jun 28;35(19):5206-15. Epub 2014 Mar 28.
School of Pharmacy, Wenzhou Medical University, Wenzhou 325035, Zhejiang, China. Electronic address:
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PLoS One 2011 6;6(6):e20669. Epub 2011 Jun 6.
School of Pharmacy and Chinese-American Research Institute for Diabetic Complications, Wenzhou Medical College, Wenzhou, Zhejiang, China.
As one of fibroblast growth factor (FGF) family members, FGF21 has been extensively investigated for its potential as a drug candidate to combat metabolic diseases. In the present study, recombinant human FGF21 (rhFGF21) was modified with polyethylene glycol (PEGylation) in order to increase its in vivo biostabilities and therapeutic potency. At N-terminal residue rhFGF21 was site-selectively PEGylated with mPEG20 kDa-butyraldehyde. Read More
PLoS One 2012 27;7(11):e49345. Epub 2012 Nov 27.
Department of Protein Sciences, Amgen Inc., Thousand Oaks, CA, USA.
Fibroblast growth factor 21 (FGF21) is a promising drug candidate for the treatment of type 2 diabetes. However, the use of wild type native FGF21 is challenging due to several limitations. Among these are its short half-life, its susceptibility to in vivo proteolytic degradation and its propensity to in vitro aggregation. Read More
Bioconjug Chem 2013 Jun 9;24(6):915-25. Epub 2013 May 9.
Department of Metabolic Disorders, Amgen Inc., One Amgen Center Drive, Thousand Oaks, California 91320, United States.
Fibroblast growth factor 21 (FGF21) is involved in regulating energy metabolism, and it has shown significant promise as a treatment for type II diabetes; however, the native protein has a very short circulating half-life necessitating frequent injections to maintain a physiological effect. Polyethylene glycol (PEG) conjugation to proteins has been used as a method for extending the circulating half-life of many pharmaceutical proteins; however, PEG does carry the risk of vacuole formation, particularly in the renal tubular epithelium. Since renal vacuole formation may be particularly problematic for diabetic patients, we engineered site-directed PEGylated variants of FGF21 with sustained potency and minimized vacuole formation. Read More
Bioconjug Chem 2012 Apr 2;23(4):740-50. Epub 2012 Apr 2.
Key Laboratory of Biotechnology and Pharmaceutical Engineering of Zhejiang Province, Wenzhou Medical College, Wenzhou 325035, China.
Recombinant fibroblast growth factor-2 (FGF-2) has been extensively studied and used in several clinical applications including wound healing, bone regeneration, and neuroprotection. Poly(ethylene glycol) (PEG) modification of recombinant human FGF-2 (rhFGF-2) in solution phase has been studied to increase the in vivo biostabilities and therapeutic potency. However, the solution-phase strategy is not site-controlled and the products are often not homogeneous due to the generation of multi-PEGylated proteins. Read More