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Artificial Affinity Proteins as Ligands of Immunoglobulins

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 specif...

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Detalles Bibliográficos
Autores principales: Mouratou, Barbara, Béhar, Ghislaine, Pecorari, Frédéric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384111/
https://www.ncbi.nlm.nih.gov/pubmed/25647098
http://dx.doi.org/10.3390/biom5010060
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author Mouratou, Barbara
Béhar, Ghislaine
Pecorari, Frédéric
author_facet Mouratou, Barbara
Béhar, Ghislaine
Pecorari, Frédéric
author_sort Mouratou, Barbara
collection PubMed
description 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.
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spelling pubmed-43841112015-05-05 Artificial Affinity Proteins as Ligands of Immunoglobulins Mouratou, Barbara Béhar, Ghislaine Pecorari, Frédéric Biomolecules Review 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. MDPI 2015-01-30 /pmc/articles/PMC4384111/ /pubmed/25647098 http://dx.doi.org/10.3390/biom5010060 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Mouratou, Barbara
Béhar, Ghislaine
Pecorari, Frédéric
Artificial Affinity Proteins as Ligands of Immunoglobulins
title Artificial Affinity Proteins as Ligands of Immunoglobulins
title_full Artificial Affinity Proteins as Ligands of Immunoglobulins
title_fullStr Artificial Affinity Proteins as Ligands of Immunoglobulins
title_full_unstemmed Artificial Affinity Proteins as Ligands of Immunoglobulins
title_short Artificial Affinity Proteins as Ligands of Immunoglobulins
title_sort artificial affinity proteins as ligands of immunoglobulins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384111/
https://www.ncbi.nlm.nih.gov/pubmed/25647098
http://dx.doi.org/10.3390/biom5010060
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