Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics. (June 2015)

• Record Type: Journal Article
• Authors: Rath, Timo; Baker, Kristi; Dumont, Jennifer A.; Peters, Robert T.; Jiang, Haiyan; Qiao, Shuo-Wang; Lencer, Wayne I.; Pierce, Glenn F.; Blumberg, Richard S.
• Is Part Of: Critical reviews in biotechnology. Volume 35:Number 2(2015:Jun.)
• Page Start: 235
• Page End: 254
• Publication Date: 2015-06
• Subjects: Biotechnology -- Periodicals; Biotechnology -- Periodicals; Review Literature -- Periodicals; Public Health -- Periodicals; Environment -- Periodicals; Industry -- Periodicals; Biotechnology; Review Literature; Public Health; Environment; Industry; 660.6
• DOI: 10.3109/07388551.2013.834293
• Languages: English
• ISSNs: 0738-8551

Abstract

<abstract> <title>Abstract</title> <p>Nearly 350 IgG-based therapeutics are approved for clinical use or are under development for many diseases lacking adequate treatment options. These include molecularly engineered biologicals comprising the IgG Fc-domain fused to various effector molecules (so-called Fc-fusion proteins) that confer the advantages of IgG, including binding to the neonatal Fc receptor (FcRn) to facilitate <italic>in vivo</italic> stability, and the therapeutic benefit of the specific effector functions. Advances in IgG structure-function relationships and an understanding of FcRn biology have provided therapeutic opportunities for previously unapproachable diseases. This article discusses approved Fc-fusion therapeutics, novel Fc-fusion proteins and FcRn-dependent delivery approaches in development, and how engineering of the FcRn–Fc interaction can generate longer-lasting and more effective therapeutics.</p> </abstract>