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Affinity-Based Methods for Site-Specific Conjugation of Antibodies

[Image: see text] Conjugation of various reagents to antibodies has long been an elegant way to combine the superior binding features of the antibody with other desired but non-natural functions. Applications range from labels for detection in different analytical assays to the creation of new drugs...

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Autores principales: von Witting, Emma, Hober, Sophia, Kanje, Sara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8377709/
https://www.ncbi.nlm.nih.gov/pubmed/34369763
http://dx.doi.org/10.1021/acs.bioconjchem.1c00313
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author von Witting, Emma
Hober, Sophia
Kanje, Sara
author_facet von Witting, Emma
Hober, Sophia
Kanje, Sara
author_sort von Witting, Emma
collection PubMed
description [Image: see text] Conjugation of various reagents to antibodies has long been an elegant way to combine the superior binding features of the antibody with other desired but non-natural functions. Applications range from labels for detection in different analytical assays to the creation of new drugs by conjugation to molecules which improves the pharmaceutical effect. In many of these applications, it has been proven advantageous to control both the site and the stoichiometry of the conjugation to achieve a homogeneous product with predictable, and often also improved, characteristics. For this purpose, many research groups have, during the latest decade, reported novel methods and techniques, based on small molecules, peptides, and proteins with inherent affinity for the antibody, for site-specific conjugation of antibodies. This review provides a comprehensive overview of these methods and their applications and also describes a historical perspective of the field.
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spelling pubmed-83777092021-08-31 Affinity-Based Methods for Site-Specific Conjugation of Antibodies von Witting, Emma Hober, Sophia Kanje, Sara Bioconjug Chem [Image: see text] Conjugation of various reagents to antibodies has long been an elegant way to combine the superior binding features of the antibody with other desired but non-natural functions. Applications range from labels for detection in different analytical assays to the creation of new drugs by conjugation to molecules which improves the pharmaceutical effect. In many of these applications, it has been proven advantageous to control both the site and the stoichiometry of the conjugation to achieve a homogeneous product with predictable, and often also improved, characteristics. For this purpose, many research groups have, during the latest decade, reported novel methods and techniques, based on small molecules, peptides, and proteins with inherent affinity for the antibody, for site-specific conjugation of antibodies. This review provides a comprehensive overview of these methods and their applications and also describes a historical perspective of the field. American Chemical Society 2021-08-09 2021-08-18 /pmc/articles/PMC8377709/ /pubmed/34369763 http://dx.doi.org/10.1021/acs.bioconjchem.1c00313 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle von Witting, Emma
Hober, Sophia
Kanje, Sara
Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title_full Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title_fullStr Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title_full_unstemmed Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title_short Affinity-Based Methods for Site-Specific Conjugation of Antibodies
title_sort affinity-based methods for site-specific conjugation of antibodies
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8377709/
https://www.ncbi.nlm.nih.gov/pubmed/34369763
http://dx.doi.org/10.1021/acs.bioconjchem.1c00313
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