Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex

Facilitated dissociation is a mechanism where antibody-mediated disruption of high-affinity complexes can enhance the therapeutic effects of a drug. Here the authors present a yeast display approach to select and engineer omalizumab variants that dissociate receptor-bound IgE to accelerate its inhib...

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Autores principales:	Luke F. Pennington, Pascal Gasser, Silke Kleinboelting, Chensong Zhang, Georgios Skiniotis, Alexander Eggel, Theodore S. Jardetzky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ce93054282b0409585dfb3dd0b17d1d1
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spelling	oai:doaj.org-article:ce93054282b0409585dfb3dd0b17d1d12021-12-05T12:22:43ZDirected evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex10.1038/s41467-021-27397-z2041-1723https://doaj.org/article/ce93054282b0409585dfb3dd0b17d1d12021-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27397-zhttps://doaj.org/toc/2041-1723Facilitated dissociation is a mechanism where antibody-mediated disruption of high-affinity complexes can enhance the therapeutic effects of a drug. Here the authors present a yeast display approach to select and engineer omalizumab variants that dissociate receptor-bound IgE to accelerate its inhibition of the allergic response.Luke F. PenningtonPascal GasserSilke KleinboeltingChensong ZhangGeorgios SkiniotisAlexander EggelTheodore S. JardetzkyNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Luke F. Pennington Pascal Gasser Silke Kleinboelting Chensong Zhang Georgios Skiniotis Alexander Eggel Theodore S. Jardetzky Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
description	Facilitated dissociation is a mechanism where antibody-mediated disruption of high-affinity complexes can enhance the therapeutic effects of a drug. Here the authors present a yeast display approach to select and engineer omalizumab variants that dissociate receptor-bound IgE to accelerate its inhibition of the allergic response.
format	article
author	Luke F. Pennington Pascal Gasser Silke Kleinboelting Chensong Zhang Georgios Skiniotis Alexander Eggel Theodore S. Jardetzky
author_facet	Luke F. Pennington Pascal Gasser Silke Kleinboelting Chensong Zhang Georgios Skiniotis Alexander Eggel Theodore S. Jardetzky
author_sort	Luke F. Pennington
title	Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
title_short	Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
title_full	Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
title_fullStr	Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
title_full_unstemmed	Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
title_sort	directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ce93054282b0409585dfb3dd0b17d1d1
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Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex

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