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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2011
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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 |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-3123181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT demarcoario biotechnologicalapplicationsofrecombinantsingledomainantibodyfragments |