Fc-fusion Proteins in Therapy: An Updated View | Bentham Science
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Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Review Article

Fc-fusion Proteins in Therapy: An Updated View

Author(s): Reza Jafari, Naime M. Zolbanin, Houshang Rafatpanah, Jafar Majidi and Tohid Kazemi*

Volume 24, Issue 12, 2017

Page: [1228 - 1237] Pages: 10

DOI: 10.2174/0929867324666170113112759

Price: $65

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Abstract

Fc-fusion proteins are composed of Fc region of IgG antibody (Hinge-CH2-CH3) and a desired linked protein. Fc region of Fc-fusion proteins can bind to neonatal Fc receptor (FcRn) thereby rescuing it from degradation. The first therapeutic Fc-fusion protein was introduced for the treatment of AIDS. The molecular designing is the first stage in production of Fc-fusion proteins. The amino acid residues in the Fc region and linked protein are very important in the bioactivity and affinity of the fusion proteins. Although, therapeutic monoclonal antibodies are the top selling biologics but the application of therapeutic Fc-fusion proteins in clinic is in progress and among these medications Etanercept is the most effective in therapy. At present, eleven Fc-fusion proteins have been approved by FDA. There are novel Fc-fusion proteins which are in pre-clinical and clinical development. In this article, we review the molecular and biological characteristics of Fc-fusion proteins and then further discuss the features of novel therapeutic Fc-fusion proteins.

Keywords: Fc-fusion proteins, immunotherapy, FcRn, antibody, Fc region.


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