Article
Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo.
Scientific reports - 20 Dec 2016
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
Abstract excerpt
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 reduced aggregation and increased serum persistence in vivo. We show that the human monoclonal antibody, MEDI1912,...
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