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      Affibody molecules as engineered protein drugs

      review-article
      1 , 2 , * , 3
      Experimental & Molecular Medicine
      Nature Publishing Group

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          Abstract

          Affibody molecules can be used as tools for molecular recognition in diagnostic and therapeutic applications. There are several preclinical studies reported on diagnostic and therapeutic use of this molecular class of alternative scaffolds, and early clinical evidence is now beginning to accumulate that suggests the Affibody molecules to be efficacious and safe in man. The small size and ease of engineering make Affibody molecules suitable for use in multispecific constructs where AffiMabs is one such that offers the option to potentiate antibodies for use in complex disease.

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          Most cited references77

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          Therapeutic strategies for the clinical blockade of IL-6/gp130 signaling.

          The successful treatment of certain autoimmune conditions with the humanized anti-IL-6 receptor (IL-6R) antibody tocilizumab has emphasized the clinical importance of cytokines that signal through the β-receptor subunit glycoprotein 130 (gp130). In this Review, we explore how gp130 signaling controls disease progression and examine why IL-6 has a special role among these cytokines as an inflammatory regulator. Attention will be given to the role of the soluble IL-6R, and we will provide a perspective into the clinical blockade of IL-6 activity in autoimmunity, inflammation, and cancer.
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            Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications.

            Affibody molecules are a class of engineered affinity proteins with proven potential for therapeutic, diagnostic and biotechnological applications. Affibody molecules are small (6.5 kDa) single domain proteins that can be isolated for high affinity and specificity to any given protein target. Fifteen years after its discovery, the Affibody technology is gaining use in many groups as a tool for creating molecular specificity wherever a small, engineering compatible tool is warranted. Here we summarize recent results using this technology, propose an Affibody nomenclature and give an overview of different HER2-specific Affibody molecules. Cumulative evidence suggests that the three helical scaffold domain used as basis for these molecules is highly suited to create a molecular affinity handle for vastly different applications. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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              Engineering novel binding proteins from nonimmunoglobulin domains.

              Not all adaptive immune systems use the immunoglobulin fold as the basis for specific recognition molecules: sea lampreys, for example, have evolved an adaptive immune system that is based on leucine-rich repeat proteins. Additionally, many other proteins, not necessarily involved in adaptive immunity, mediate specific high-affinity interactions. Such alternatives to immunoglobulins represent attractive starting points for the design of novel binding molecules for research and clinical applications. Indeed, through progress and increased experience in library design and selection technologies, gained not least from working with synthetic antibody libraries, researchers have now exploited many of these novel scaffolds as tailor-made affinity reagents. Significant progress has been made not only in the basic science of generating specific binding molecules, but also in applications of the selected binders in laboratory procedures, proteomics, diagnostics and therapy. Challenges ahead include identifying applications where these novel proteins can not only be an alternative, but can enable approaches so far deemed technically impossible, and delineate those therapeutic applications commensurate with the molecular properties of the respective proteins.
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                Author and article information

                Journal
                Exp Mol Med
                Exp. Mol. Med
                Experimental & Molecular Medicine
                Nature Publishing Group
                1226-3613
                2092-6413
                March 2017
                24 March 2017
                1 March 2017
                : 49
                : 3
                : e306
                Affiliations
                [1 ]Affibody AB , Solna, Sweden
                [2 ]Department of Immunology, Genetics and Pathology, Uppsala University , Uppsala, Sweden
                [3 ]AbClon Inc. , Guro-gu, Seoul, Republic of Korea
                Author notes
                [* ]Affibody AB , Gunnar Asplunds Allé 24, Solna, SE-171 69, Sweden. E-mail: fredrik.frejd@ 123456affibody.com
                Article
                emm201735
                10.1038/emm.2017.35
                5382565
                28336959
                e1cb40e3-c6fd-4a04-b107-05f2bd3e68ab
                Copyright © 2017 The Author(s)

                This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

                History
                : 07 December 2016
                : 22 December 2016
                Categories
                Review

                Molecular medicine
                Molecular medicine

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