author_facet Li, Zeyang
Theile, Christopher S.
Chen, Guan‐Yu
Bilate, Angelina M.
Duarte, Joao N.
Avalos, Ana M.
Fang, Tao
Barberena, Roberto
Sato, Shuji
Ploegh, Hidde L.
Li, Zeyang
Theile, Christopher S.
Chen, Guan‐Yu
Bilate, Angelina M.
Duarte, Joao N.
Avalos, Ana M.
Fang, Tao
Barberena, Roberto
Sato, Shuji
Ploegh, Hidde L.
author Li, Zeyang
Theile, Christopher S.
Chen, Guan‐Yu
Bilate, Angelina M.
Duarte, Joao N.
Avalos, Ana M.
Fang, Tao
Barberena, Roberto
Sato, Shuji
Ploegh, Hidde L.
spellingShingle Li, Zeyang
Theile, Christopher S.
Chen, Guan‐Yu
Bilate, Angelina M.
Duarte, Joao N.
Avalos, Ana M.
Fang, Tao
Barberena, Roberto
Sato, Shuji
Ploegh, Hidde L.
Angewandte Chemie International Edition
Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
General Chemistry
Catalysis
author_sort li, zeyang
spelling Li, Zeyang Theile, Christopher S. Chen, Guan‐Yu Bilate, Angelina M. Duarte, Joao N. Avalos, Ana M. Fang, Tao Barberena, Roberto Sato, Shuji Ploegh, Hidde L. 1433-7851 1521-3773 Wiley General Chemistry Catalysis http://dx.doi.org/10.1002/anie.201505277 <jats:title>Abstract</jats:title><jats:p>The site‐specific modification of proteins with fluorophores can render a protein fluorescent without compromising its function. To avoid self‐quenching from multiple fluorophores installed in close proximity, we used Holliday junctions to label proteins site‐specifically. Holliday junctions enable modification with multiple fluorophores at reasonably precise spacing. We designed a Holliday junction with three of its four arms modified with a fluorophore of choice and the remaining arm equipped with a dibenzocyclooctyne substituent to render it reactive with an azide‐modified fluorescent single‐domain antibody fragment or an intact immunoglobulin produced in a sortase‐catalyzed reaction. These fluorescent Holliday junctions improve fluorescence yields for both single‐domain and full‐sized antibodies without deleterious effects on antigen binding.</jats:p> Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments Angewandte Chemie International Edition
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title Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_unstemmed Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_full Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_fullStr Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_full_unstemmed Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_short Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_sort fluorophore‐conjugated holliday junctions for generating super‐bright antibodies and antibody fragments
topic General Chemistry
Catalysis
url http://dx.doi.org/10.1002/anie.201505277
publishDate 2015
physical 11706-11710
description <jats:title>Abstract</jats:title><jats:p>The site‐specific modification of proteins with fluorophores can render a protein fluorescent without compromising its function. To avoid self‐quenching from multiple fluorophores installed in close proximity, we used Holliday junctions to label proteins site‐specifically. Holliday junctions enable modification with multiple fluorophores at reasonably precise spacing. We designed a Holliday junction with three of its four arms modified with a fluorophore of choice and the remaining arm equipped with a dibenzocyclooctyne substituent to render it reactive with an azide‐modified fluorescent single‐domain antibody fragment or an intact immunoglobulin produced in a sortase‐catalyzed reaction. These fluorescent Holliday junctions improve fluorescence yields for both single‐domain and full‐sized antibodies without deleterious effects on antigen binding.</jats:p>
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author Li, Zeyang, Theile, Christopher S., Chen, Guan‐Yu, Bilate, Angelina M., Duarte, Joao N., Avalos, Ana M., Fang, Tao, Barberena, Roberto, Sato, Shuji, Ploegh, Hidde L.
author_facet Li, Zeyang, Theile, Christopher S., Chen, Guan‐Yu, Bilate, Angelina M., Duarte, Joao N., Avalos, Ana M., Fang, Tao, Barberena, Roberto, Sato, Shuji, Ploegh, Hidde L., Li, Zeyang, Theile, Christopher S., Chen, Guan‐Yu, Bilate, Angelina M., Duarte, Joao N., Avalos, Ana M., Fang, Tao, Barberena, Roberto, Sato, Shuji, Ploegh, Hidde L.
author_sort li, zeyang
container_issue 40
container_start_page 11706
container_title Angewandte Chemie International Edition
container_volume 54
description <jats:title>Abstract</jats:title><jats:p>The site‐specific modification of proteins with fluorophores can render a protein fluorescent without compromising its function. To avoid self‐quenching from multiple fluorophores installed in close proximity, we used Holliday junctions to label proteins site‐specifically. Holliday junctions enable modification with multiple fluorophores at reasonably precise spacing. We designed a Holliday junction with three of its four arms modified with a fluorophore of choice and the remaining arm equipped with a dibenzocyclooctyne substituent to render it reactive with an azide‐modified fluorescent single‐domain antibody fragment or an intact immunoglobulin produced in a sortase‐catalyzed reaction. These fluorescent Holliday junctions improve fluorescence yields for both single‐domain and full‐sized antibodies without deleterious effects on antigen binding.</jats:p>
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spelling Li, Zeyang Theile, Christopher S. Chen, Guan‐Yu Bilate, Angelina M. Duarte, Joao N. Avalos, Ana M. Fang, Tao Barberena, Roberto Sato, Shuji Ploegh, Hidde L. 1433-7851 1521-3773 Wiley General Chemistry Catalysis http://dx.doi.org/10.1002/anie.201505277 <jats:title>Abstract</jats:title><jats:p>The site‐specific modification of proteins with fluorophores can render a protein fluorescent without compromising its function. To avoid self‐quenching from multiple fluorophores installed in close proximity, we used Holliday junctions to label proteins site‐specifically. Holliday junctions enable modification with multiple fluorophores at reasonably precise spacing. We designed a Holliday junction with three of its four arms modified with a fluorophore of choice and the remaining arm equipped with a dibenzocyclooctyne substituent to render it reactive with an azide‐modified fluorescent single‐domain antibody fragment or an intact immunoglobulin produced in a sortase‐catalyzed reaction. These fluorescent Holliday junctions improve fluorescence yields for both single‐domain and full‐sized antibodies without deleterious effects on antigen binding.</jats:p> Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments Angewandte Chemie International Edition
spellingShingle Li, Zeyang, Theile, Christopher S., Chen, Guan‐Yu, Bilate, Angelina M., Duarte, Joao N., Avalos, Ana M., Fang, Tao, Barberena, Roberto, Sato, Shuji, Ploegh, Hidde L., Angewandte Chemie International Edition, Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments, General Chemistry, Catalysis
title Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_full Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_fullStr Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_full_unstemmed Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_short Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
title_sort fluorophore‐conjugated holliday junctions for generating super‐bright antibodies and antibody fragments
title_unstemmed Fluorophore‐Conjugated Holliday Junctions for Generating Super‐Bright Antibodies and Antibody Fragments
topic General Chemistry, Catalysis
url http://dx.doi.org/10.1002/anie.201505277