Abstract
Fc-fusion proteins have been successfully implemented in the treatment of many diseases. Advances in engineering and design of these therapeutic proteins have helped prolong the drug half-life, which in turn allows for longer dosing intervals (i.e. weekly or bi-weekly administration) and, thus, may improve patient adherence in a real world setting. In this review, we provide a brief summary of half-life extension technologies. Here, we focus on IgG-Fc fusion and the key roles that the Fc fragment plays in both physiology and drug therapy, and the potential to elicit immune responses in humans. This review provides examples of various recombinant Fc-fusion protein drugs, including, etanercept (Enbrel®) for the treatment of various forms of arthritis, aflibercept (Eylea®), for the treatment of neovascular age-related macular degeneration and dulaglutide (Trulicity™) for the treatment of type 2 diabetes. All of these fusion proteins can be administered at least weekly. Overall, Fc-fusion proteins have proven to be a successful alternative to improve pharmacological properties of therapeutic drugs, with more convenient utilization in the real world and with low immunogenic potential.
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