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Homogeneous Bispecifics by Disulfide Bridging
[Image: see text] We report on a chemical platform to generate site-specific, homogeneous, antibody–antibody conjugates by targeting and bridging disulfide bonds. A bispecific antibody construct was produced in good yield through simple reduction and bridging of antibody fragment disulfide bonds, us...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4458859/ https://www.ncbi.nlm.nih.gov/pubmed/25033024 http://dx.doi.org/10.1021/bc5002467 |
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author | Hull, Elizabeth A. Livanos, Maria Miranda, Enrique Smith, Mark E. B. Chester, Kerry A. Baker, James R. |
author_facet | Hull, Elizabeth A. Livanos, Maria Miranda, Enrique Smith, Mark E. B. Chester, Kerry A. Baker, James R. |
author_sort | Hull, Elizabeth A. |
collection | PubMed |
description | [Image: see text] We report on a chemical platform to generate site-specific, homogeneous, antibody–antibody conjugates by targeting and bridging disulfide bonds. A bispecific antibody construct was produced in good yield through simple reduction and bridging of antibody fragment disulfide bonds, using a readily synthesized bis-dibromomaleimide cross-linker. Binding activity of antibodies was maintained, and in vitro binding of target antigens was observed. This technology is demonstrated through linking scFv and Fab antibody fragments, showing its potential for the construction of a diverse range of bispecifics. |
format | Online Article Text |
id | pubmed-4458859 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-44588592015-06-11 Homogeneous Bispecifics by Disulfide Bridging Hull, Elizabeth A. Livanos, Maria Miranda, Enrique Smith, Mark E. B. Chester, Kerry A. Baker, James R. Bioconjug Chem [Image: see text] We report on a chemical platform to generate site-specific, homogeneous, antibody–antibody conjugates by targeting and bridging disulfide bonds. A bispecific antibody construct was produced in good yield through simple reduction and bridging of antibody fragment disulfide bonds, using a readily synthesized bis-dibromomaleimide cross-linker. Binding activity of antibodies was maintained, and in vitro binding of target antigens was observed. This technology is demonstrated through linking scFv and Fab antibody fragments, showing its potential for the construction of a diverse range of bispecifics. American Chemical Society 2014-07-17 2014-08-20 /pmc/articles/PMC4458859/ /pubmed/25033024 http://dx.doi.org/10.1021/bc5002467 Text en Copyright © 2014 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. |
spellingShingle | Hull, Elizabeth A. Livanos, Maria Miranda, Enrique Smith, Mark E. B. Chester, Kerry A. Baker, James R. Homogeneous Bispecifics by Disulfide Bridging |
title | Homogeneous
Bispecifics by Disulfide Bridging |
title_full | Homogeneous
Bispecifics by Disulfide Bridging |
title_fullStr | Homogeneous
Bispecifics by Disulfide Bridging |
title_full_unstemmed | Homogeneous
Bispecifics by Disulfide Bridging |
title_short | Homogeneous
Bispecifics by Disulfide Bridging |
title_sort | homogeneous
bispecifics by disulfide bridging |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4458859/ https://www.ncbi.nlm.nih.gov/pubmed/25033024 http://dx.doi.org/10.1021/bc5002467 |
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