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Biotechnological applications of recombinant single-domain antibody fragments

BACKGROUND: Single-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications. RESULT...

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Detalles Bibliográficos
Autor principal: de Marco, Ario
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3123181/
https://www.ncbi.nlm.nih.gov/pubmed/21658216
http://dx.doi.org/10.1186/1475-2859-10-44
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author de Marco, Ario
author_facet de Marco, Ario
author_sort de Marco, Ario
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description BACKGROUND: Single-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications. RESULTS: The discovery of the single-domain antibody's potentials has stimulated their use in an increasing variety of fields. The rapid accumulation of articles describing new applications and further developments of established approaches has made it, therefore, necessary to update the previous reviews with a new and more complete summary of the topic. CONCLUSIONS: Beside the necessary task of updating, this work analyses in detail some applicative aspects of the single-domain antibodies that have been overseen in the past, such as their efficacy in affinity chromatography, as co-crystallization chaperones, protein aggregation controllers, enzyme activity tuners, and the specificities of the unconventional single-domain fragments.
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spelling pubmed-31231812011-06-25 Biotechnological applications of recombinant single-domain antibody fragments de Marco, Ario Microb Cell Fact Review BACKGROUND: Single-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications. RESULTS: The discovery of the single-domain antibody's potentials has stimulated their use in an increasing variety of fields. The rapid accumulation of articles describing new applications and further developments of established approaches has made it, therefore, necessary to update the previous reviews with a new and more complete summary of the topic. CONCLUSIONS: Beside the necessary task of updating, this work analyses in detail some applicative aspects of the single-domain antibodies that have been overseen in the past, such as their efficacy in affinity chromatography, as co-crystallization chaperones, protein aggregation controllers, enzyme activity tuners, and the specificities of the unconventional single-domain fragments. BioMed Central 2011-06-09 /pmc/articles/PMC3123181/ /pubmed/21658216 http://dx.doi.org/10.1186/1475-2859-10-44 Text en Copyright ©2011 de Marco; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
de Marco, Ario
Biotechnological applications of recombinant single-domain antibody fragments
title Biotechnological applications of recombinant single-domain antibody fragments
title_full Biotechnological applications of recombinant single-domain antibody fragments
title_fullStr Biotechnological applications of recombinant single-domain antibody fragments
title_full_unstemmed Biotechnological applications of recombinant single-domain antibody fragments
title_short Biotechnological applications of recombinant single-domain antibody fragments
title_sort biotechnological applications of recombinant single-domain antibody fragments
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3123181/
https://www.ncbi.nlm.nih.gov/pubmed/21658216
http://dx.doi.org/10.1186/1475-2859-10-44
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