Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo

Uncontrolled self-association is a major challenge in the exploitation of proteins as therapeutics. Here we describe the development of a structural proteomics approach to identify the amino acids responsible for aberrant self-association of monoclonal antibodies and the design of a variant with red...

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Detalles Bibliográficos
Autores principales: Dobson, Claire L., Devine, Paul W. A., Phillips, Jonathan J., Higazi, Daniel R., Lloyd, Christopher, Popovic, Bojana, Arnold, Joanne, Buchanan, Andrew, Lewis, Arthur, Goodman, Joanne, van der Walle, Christopher F., Thornton, Peter, Vinall, Lisa, Lowne, David, Aagaard, Anna, Olsson, Lise-Lotte, Ridderstad Wollberg, Anna, Welsh, Fraser, Karamanos, Theodoros K., Pashley, Clare L., Iadanza, Matthew G., Ranson, Neil A., Ashcroft, Alison E., Kippen, Alistair D., Vaughan, Tristan J., Radford, Sheena E., Lowe, David C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171805/
https://www.ncbi.nlm.nih.gov/pubmed/27995962
http://dx.doi.org/10.1038/srep38644

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5171805/
https://www.ncbi.nlm.nih.gov/pubmed/27995962
http://dx.doi.org/10.1038/srep38644

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