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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...

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Autores principales: Hull, Elizabeth A., Livanos, Maria, Miranda, Enrique, Smith, Mark E. B., Chester, Kerry A., Baker, James R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
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.
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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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