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Biomolecules 2015, 5(1), 60-75; doi:10.3390/biom5010060

Artificial Affinity Proteins as Ligands of Immunoglobulins

1
INSERM UMR 892 - CRCNA, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France
2
CNRS UMR 6299, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France
3
University of Nantes, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France
*
Authors to whom correspondence should be addressed.
Received: 13 November 2014 / Revised: 17 December 2014 / Accepted: 23 January 2015 / Published: 30 January 2015
(This article belongs to the Special Issue Immunoglobulin)
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Abstract

A number of natural proteins are known to have affinity and specificity for immunoglobulins. Some of them are widely used as reagents for detection or capture applications, such as Protein G and Protein A. However, these natural proteins have a defined spectrum of recognition that may not fit specific needs. With the development of combinatorial protein engineering and selection techniques, it has become possible to design artificial affinity proteins with the desired properties. These proteins, termed alternative scaffold proteins, are most often chosen for their stability, ease of engineering and cost-efficient recombinant production in bacteria. In this review, we focus on alternative scaffold proteins for which immunoglobulin binders have been identified and characterized. View Full-Text
Keywords: immunoglobulin; Fc; alternative scaffold protein; Affibody; Affitin; DARPin; monobody; knottin; CBM immunoglobulin; Fc; alternative scaffold protein; Affibody; Affitin; DARPin; monobody; knottin; CBM
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Mouratou, B.; Béhar, G.; Pecorari, F. Artificial Affinity Proteins as Ligands of Immunoglobulins. Biomolecules 2015, 5, 60-75.

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